D00234
type: Enzyme
rlcp: p463
cath: Elastase; domain 1
cath: Neutral Protease; domain 2
ec: https://purl.uniprot.org/enzyme/3.4.24.27
csa: 1tlp
csa: 8tln
macie: M0176
uniprot: P00800
kegg enzyme: thermolysin
kegg cofactor: Zinc
kegg substrate: Protein
kegg substrate: Peptide
kegg substrate: H2O
kegg product: Protein
kegg product: Peptide
pdb: 1fj3A01
pdb: 1fjoA01
pdb: 1fjqA01
pdb: 1fjtA01
pdb: 1fjuA01
pdb: 1fjvA01
pdb: 1fjwA01
pdb: 1gxwA01
pdb: 1hytA01
pdb: 1keiA01
pdb: 1kjoA01
pdb: 1kjpA01
pdb: 1kkkA01
pdb: 1kl6A01
pdb: 1kr6A01
pdb: 1kroA01
pdb: 1ks7A01
pdb: 1ktoA01
pdb: 1l3fE01
pdb: 1lnaE01
pdb: 1lnbE01
pdb: 1lncE01
pdb: 1lndE01
pdb: 1lneE01
pdb: 1lnfE01
pdb: 1os0A01
pdb: 1qf0A01
pdb: 1qf1A01
pdb: 1qf2A01
pdb: 1thlA01
pdb: 1tliA01
pdb: 1tlpE01
pdb: 1tlxA01
pdb: 1tmnE01
pdb: 2tliA01
pdb: 2tlxA01
pdb: 2tmnE01
pdb: 3tliA01
pdb: 3tlnA01
pdb: 3tmnE01
pdb: 4tliA01
pdb: 4tlnA01
pdb: 4tmnE01
pdb: 5tliA01
pdb: 5tlnA01
pdb: 5tmnE01
pdb: 6tliA01
pdb: 6tmnE01
pdb: 7tliA01
pdb: 7tlnA01
pdb: 8tliA01
pdb: 8tlnE01
pdb: 1fj3A02
pdb: 1fjoA02
pdb: 1fjqA02
pdb: 1fjtA02
pdb: 1fjuA02
pdb: 1fjvA02
pdb: 1fjwA02
pdb: 1gxwA02
pdb: 1hytA02
pdb: 1keiA02
pdb: 1kjoA02
pdb: 1kjpA02

Elastase; domain 1
type: Cath
references: http://www.cathdb.info/version/latest/superfamily/3.10.170.10
catalytic domain: index.html

Neutral Protease; domain 2
type: Cath
references: http://www.cathdb.info/version/latest/superfamily/1.10.390.10
catalytic domain: index.html

Zinc
type: KeggCofactor
references: KEGG:C00038
compound type: heavy metal
references: CHEBI:29105
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

Protein
type: KeggSubstrate
references: KEGG:C00017
compound type: peptide/protein
type: KeggProduct

Peptide
type: KeggSubstrate
references: KEGG:C00012
compound type: peptide/protein
type: KeggProduct
label: Peptide(leaving group)

H2O
type: KeggSubstrate
references: KEGG:C00001
compound type: H2O
references: CHEBI:15377
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

1fj3A01
type: Pdb
references: 1fj3
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1fj3
catalytic residue: ASN 112;GLU 143
cofactor binding residue: HIS 142;HIS 146(Zinc binding)
main chain in catalysis: ALA 113

1fjoA01
type: Pdb
references: 1fjo
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1fjo
catalytic residue: ASN 112;GLU 143
cofactor binding residue: HIS 142;HIS 146(Zinc binding)
main chain in catalysis: ALA 113

1fjqA01
type: Pdb
references: 1fjq
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1fjq
catalytic residue: ASN 112;GLU 143
cofactor binding residue: HIS 142;HIS 146(Zinc binding)
main chain in catalysis: ALA 113

1fjtA01
type: Pdb
references: 1fjt
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1fjt
catalytic residue: ASN 112;GLU 143
cofactor binding residue: HIS 142;HIS 146(Zinc binding)
main chain in catalysis: ALA 113

1fjuA01
type: Pdb
references: 1fju
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1fju
catalytic residue: ASN 112;GLU 143
cofactor binding residue: HIS 142;HIS 146(Zinc binding)
main chain in catalysis: ALA 113

1fjvA01
type: Pdb
references: 1fjv
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1fjv
catalytic residue: ASN 112;GLU 143
cofactor binding residue: HIS 142;HIS 146(Zinc binding)
main chain in catalysis: ALA 113

1fjwA01
type: Pdb
references: 1fjw
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1fjw
catalytic residue: ASN 112;GLU 143
cofactor binding residue: HIS 142;HIS 146(Zinc binding)
main chain in catalysis: ALA 113

1gxwA01
type: Pdb
references: 1gxw
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1gxw
catalytic residue: ASN 112;GLU 143
cofactor binding residue: HIS 142;HIS 146(Zinc binding)
main chain in catalysis: ALA 113

1hytA01
type: Pdb
references: 1hyt
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1hyt
catalytic residue: ASN 112;GLU 143
cofactor binding residue: HIS 142;HIS 146(Zinc binding)
main chain in catalysis: ALA 113

1keiA01
type: Pdb
references: 1kei
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1kei
catalytic residue: ASN 112;GLU 143
cofactor binding residue: HIS 142;HIS 146(Zinc binding)
main chain in catalysis: ALA 113

1kjoA01
type: Pdb
references: 1kjo
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1kjo
catalytic residue: ASN 112;GLU 143
cofactor binding residue: HIS 142;HIS 146(Zinc binding)
main chain in catalysis: ALA 113

1kjpA01
type: Pdb
references: 1kjp
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1kjp
catalytic residue: ASN 112;GLU 143
cofactor binding residue: HIS 142;HIS 146(Zinc binding)
main chain in catalysis: ALA 113

1kkkA01
type: Pdb
references: 1kkk
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1kkk
catalytic residue: ASN 112;GLU 143
cofactor binding residue: HIS 142;HIS 146(Zinc binding)
main chain in catalysis: ALA 113

1kl6A01
type: Pdb
references: 1kl6
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1kl6
catalytic residue: ASN 112;GLU 143
cofactor binding residue: HIS 142;HIS 146(Zinc binding)
main chain in catalysis: ALA 113

1kr6A01
type: Pdb
references: 1kr6
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1kr6
catalytic residue: ASN 112;GLU 143
cofactor binding residue: HIS 142;HIS 146(Zinc binding)
main chain in catalysis: ALA 113

1kroA01
type: Pdb
references: 1kro
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1kro
catalytic residue: ASN 112;GLU 143
cofactor binding residue: HIS 142;HIS 146(Zinc binding)
main chain in catalysis: ALA 113

1ks7A01
type: Pdb
references: 1ks7
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ks7
catalytic residue: ASN 112;GLU 143
cofactor binding residue: HIS 142;HIS 146(Zinc binding)
main chain in catalysis: ALA 113

1ktoA01
type: Pdb
references: 1kto
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1kto
catalytic residue: ASN 112;GLU 143
cofactor binding residue: HIS 142;HIS 146(Zinc binding)
main chain in catalysis: ALA 113

1l3fE01
type: Pdb
references: 1l3f
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1l3f
catalytic residue: ASN 112;GLU 143
cofactor binding residue: HIS 142;HIS 146(Zinc binding)
main chain in catalysis: ALA 113

1lnaE01
type: Pdb
references: 1lna
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1lna
catalytic residue: ASN 112;GLU 143
cofactor binding residue: HIS 142;HIS 146(Zinc binding)
main chain in catalysis: ALA 113

1lnbE01
type: Pdb
references: 1lnb
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1lnb
catalytic residue: ASN 112;GLU 143
cofactor binding residue: HIS 142;HIS 146(Zinc binding)
main chain in catalysis: ALA 113

1lncE01
type: Pdb
references: 1lnc
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1lnc
catalytic residue: ASN 112;GLU 143
cofactor binding residue: HIS 142;HIS 146(Zinc binding)
main chain in catalysis: ALA 113

1lndE01
type: Pdb
references: 1lnd
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1lnd
catalytic residue: ASN 112;GLU 143
cofactor binding residue: HIS 142;HIS 146(Zinc binding)
main chain in catalysis: ALA 113

1lneE01
type: Pdb
references: 1lne
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1lne
catalytic residue: ASN 112;GLU 143
cofactor binding residue: HIS 142;HIS 146(Zinc binding)
main chain in catalysis: ALA 113

1lnfE01
type: Pdb
references: 1lnf
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1lnf
catalytic residue: ASN 112;GLU 143
cofactor binding residue: HIS 142;HIS 146(Zinc binding)
main chain in catalysis: ALA 113

1os0A01
type: Pdb
references: 1os0
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1os0
catalytic residue: ASN 112;GLU 143
cofactor binding residue: HIS 142;HIS 146(Zinc binding)
main chain in catalysis: ALA 113

1qf0A01
type: Pdb
references: 1qf0
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1qf0
catalytic residue: ASN 112;GLU 143
cofactor binding residue: HIS 142;HIS 146(Zinc binding)
main chain in catalysis: ALA 113

1qf1A01
type: Pdb
references: 1qf1
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1qf1
catalytic residue: ASN 112;GLU 143
cofactor binding residue: HIS 142;HIS 146(Zinc binding)
main chain in catalysis: ALA 113

1qf2A01
type: Pdb
references: 1qf2
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1qf2
catalytic residue: ASN 112;GLU 143
cofactor binding residue: HIS 142;HIS 146(Zinc binding)
main chain in catalysis: ALA 113

1thlA01
type: Pdb
references: 1thl
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1thl
catalytic residue: ASN 112;GLU 143
cofactor binding residue: HIS 142;HIS 146(Zinc binding)
main chain in catalysis: ALA 113

1tliA01
type: Pdb
references: 1tli
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1tli
catalytic residue: ASN 112;GLU 143
cofactor binding residue: HIS 142;HIS 146(Zinc binding)
main chain in catalysis: ALA 113

1tlpE01
type: Pdb
references: 1tlp
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1tlp
catalytic residue: ASN 112;GLU 143
cofactor binding residue: HIS 142;HIS 146(Zinc binding)
main chain in catalysis: ALA 113

1tlxA01
type: Pdb
references: 1tlx
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1tlx
catalytic residue: ASN 112;GLU 143
cofactor binding residue: HIS 142;HIS 146(Zinc binding)
main chain in catalysis: ALA 113

1tmnE01
type: Pdb
references: 1tmn
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1tmn
catalytic residue: ASN 112;GLU 143
cofactor binding residue: HIS 142;HIS 146(Zinc binding)
main chain in catalysis: ALA 113

2tliA01
type: Pdb
references: 2tli
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2tli
catalytic residue: ASN 112;GLU 143
cofactor binding residue: HIS 142;HIS 146(Zinc binding)
main chain in catalysis: ALA 113

2tlxA01
type: Pdb
references: 2tlx
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2tlx
catalytic residue: ASN 112;GLU 143
cofactor binding residue: HIS 142;HIS 146(Zinc binding)
main chain in catalysis: ALA 113

2tmnE01
type: Pdb
references: 2tmn
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2tmn
catalytic residue: ASN 112;GLU 143
cofactor binding residue: HIS 142;HIS 146(Zinc binding)
main chain in catalysis: ALA 113

3tliA01
type: Pdb
references: 3tli
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3tli
catalytic residue: ASN 112;GLU 143
cofactor binding residue: HIS 142;HIS 146(Zinc binding)
main chain in catalysis: ALA 113

3tlnA01
type: Pdb
references: 3tln
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3tln
catalytic residue: ASN 112;GLU 143
cofactor binding residue: HIS 142;HIS 146(Zinc binding)
main chain in catalysis: ALA 113

3tmnE01
type: Pdb
references: 3tmn
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3tmn
catalytic residue: ASN 112;GLU 143
cofactor binding residue: HIS 142;HIS 146(Zinc binding)
main chain in catalysis: ALA 113

4tliA01
type: Pdb
references: 4tli
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:4tli
catalytic residue: ASN 112;GLU 143
cofactor binding residue: HIS 142;HIS 146(Zinc binding)
main chain in catalysis: ALA 113

4tlnA01
type: Pdb
references: 4tln
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:4tln
catalytic residue: ASN 112;GLU 143
cofactor binding residue: HIS 142;HIS 146(Zinc binding)
main chain in catalysis: ALA 113

4tmnE01
type: Pdb
references: 4tmn
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:4tmn
catalytic residue: ASN 112;GLU 143
cofactor binding residue: HIS 142;HIS 146(Zinc binding)
main chain in catalysis: ALA 113

5tliA01
type: Pdb
references: 5tli
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:5tli
catalytic residue: ASN 112;GLU 143
cofactor binding residue: HIS 142;HIS 146(Zinc binding)
main chain in catalysis: ALA 113

5tlnA01
type: Pdb
references: 5tln
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:5tln
catalytic residue: ASN 112;GLU 143
cofactor binding residue: HIS 142;HIS 146(Zinc binding)
main chain in catalysis: ALA 113

5tmnE01
type: Pdb
references: 5tmn
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:5tmn
catalytic residue: ASN 112;GLU 143
cofactor binding residue: HIS 142;HIS 146(Zinc binding)
main chain in catalysis: ALA 113

6tliA01
type: Pdb
references: 6tli
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:6tli
catalytic residue: ASN 112;GLU 143
cofactor binding residue: HIS 142;HIS 146(Zinc binding)
main chain in catalysis: ALA 113

6tmnE01
type: Pdb
references: 6tmn
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:6tmn
catalytic residue: ASN 112;GLU 143
cofactor binding residue: HIS 142;HIS 146(Zinc binding)
main chain in catalysis: ALA 113

7tliA01
type: Pdb
references: 7tli
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:7tli
catalytic residue: ASN 112;GLU 143
cofactor binding residue: HIS 142;HIS 146(Zinc binding)
main chain in catalysis: ALA 113

7tlnA01
type: Pdb
references: 7tln
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:7tln
catalytic residue: ASN 112;GLU 143
cofactor binding residue: HIS 142;HIS 146(Zinc binding)
main chain in catalysis: ALA 113

8tliA01
type: Pdb
references: 8tli
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:8tli
catalytic residue: ASN 112;GLU 143
cofactor binding residue: HIS 142;HIS 146(Zinc binding)
main chain in catalysis: ALA 113

8tlnE01
type: Pdb
references: 8tln
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:8tln
catalytic residue: ASN 112;GLU 143
cofactor binding residue: HIS 142;HIS 146(Zinc binding)
main chain in catalysis: ALA 113

1fj3A02
type: Pdb
references: 1fj3
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1fj3
catalytic residue: TYR 157;HIS 231
cofactor binding residue: GLU 166(Zinc binding)

1fjoA02
type: Pdb
references: 1fjo
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1fjo
catalytic residue: TYR 157;HIS 231
cofactor binding residue: GLU 166(Zinc binding)

1fjqA02
type: Pdb
references: 1fjq
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1fjq
catalytic residue: TYR 157;HIS 231
cofactor binding residue: GLU 166(Zinc binding)

1fjtA02
type: Pdb
references: 1fjt
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1fjt
catalytic residue: TYR 157;HIS 231
cofactor binding residue: GLU 166(Zinc binding)

1fjuA02
type: Pdb
references: 1fju
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1fju
catalytic residue: TYR 157;HIS 231
cofactor binding residue: GLU 166(Zinc binding)

1fjvA02
type: Pdb
references: 1fjv
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1fjv
catalytic residue: TYR 157;HIS 231
cofactor binding residue: GLU 166(Zinc binding)

1fjwA02
type: Pdb
references: 1fjw
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1fjw
catalytic residue: TYR 157;HIS 231
cofactor binding residue: GLU 166(Zinc binding)

1gxwA02
type: Pdb
references: 1gxw
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1gxw
catalytic residue: TYR 157;HIS 231
cofactor binding residue: GLU 166(Zinc binding)

1hytA02
type: Pdb
references: 1hyt
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1hyt
catalytic residue: TYR 157;HIS 231
cofactor binding residue: GLU 166(Zinc binding)

1keiA02
type: Pdb
references: 1kei
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1kei
catalytic residue: TYR 157;HIS 231
cofactor binding residue: GLU 166(Zinc binding)

1kjoA02
type: Pdb
references: 1kjo
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1kjo
catalytic residue: TYR 157;HIS 231
cofactor binding residue: GLU 166(Zinc binding)

1kjpA02
type: Pdb
references: 1kjp
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1kjp
catalytic residue: TYR 157;HIS 231
cofactor binding residue: GLU 166(Zinc binding)

1kkkA02
type: Pdb
references: 1kkk
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1kkk
catalytic residue: TYR 157;HIS 231
cofactor binding residue: GLU 166(Zinc binding)

1kl6A02
type: Pdb
references: 1kl6
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1kl6
catalytic residue: TYR 157;HIS 231
cofactor binding residue: GLU 166(Zinc binding)

1kr6A02
type: Pdb
references: 1kr6
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1kr6
catalytic residue: TYR 157;HIS 231
cofactor binding residue: GLU 166(Zinc binding)

1kroA02
type: Pdb
references: 1kro
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1kro
catalytic residue: TYR 157;HIS 231
cofactor binding residue: GLU 166(Zinc binding)

1ks7A02
type: Pdb
references: 1ks7
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ks7
catalytic residue: TYR 157;HIS 231
cofactor binding residue: GLU 166(Zinc binding)

1ktoA02
type: Pdb
references: 1kto
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1kto
catalytic residue: TYR 157;HIS 231
cofactor binding residue: GLU 166(Zinc binding)

1l3fE02
type: Pdb
references: 1l3f
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1l3f
catalytic residue: TYR 157;HIS 231
cofactor binding residue: GLU 166(Zinc binding)

1lnaE02
type: Pdb
references: 1lna
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1lna
catalytic residue: TYR 157;HIS 231
cofactor binding residue: GLU 166(Zinc binding)

1lnbE02
type: Pdb
references: 1lnb
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1lnb
catalytic residue: TYR 157;HIS 231
cofactor binding residue: GLU 166(Zinc binding)

1lncE02
type: Pdb
references: 1lnc
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1lnc
catalytic residue: TYR 157;HIS 231
cofactor binding residue: GLU 166(Zinc binding)

1lndE02
type: Pdb
references: 1lnd
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1lnd
catalytic residue: TYR 157;HIS 231
cofactor binding residue: GLU 166(Zinc binding)

1lneE02
type: Pdb
references: 1lne
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1lne
catalytic residue: TYR 157;HIS 231
cofactor binding residue: GLU 166(Zinc binding)

1lnfE02
type: Pdb
references: 1lnf
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1lnf
catalytic residue: TYR 157;HIS 231
cofactor binding residue: GLU 166(Zinc binding)

1os0A02
type: Pdb
references: 1os0
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1os0
catalytic residue: TYR 157;HIS 231
cofactor binding residue: GLU 166(Zinc binding)

1qf0A02
type: Pdb
references: 1qf0
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1qf0
catalytic residue: TYR 157;HIS 231
cofactor binding residue: GLU 166(Zinc binding)

1qf1A02
type: Pdb
references: 1qf1
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1qf1
catalytic residue: TYR 157;HIS 231
cofactor binding residue: GLU 166(Zinc binding)

1qf2A02
type: Pdb
references: 1qf2
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1qf2
catalytic residue: TYR 157;HIS 231
cofactor binding residue: GLU 166(Zinc binding)

1thlA02
type: Pdb
references: 1thl
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1thl
catalytic residue: TYR 157;HIS 231
cofactor binding residue: GLU 166(Zinc binding)

1tliA02
type: Pdb
references: 1tli
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1tli
catalytic residue: TYR 157;HIS 231
cofactor binding residue: GLU 166(Zinc binding)

1tlpE02
type: Pdb
references: 1tlp
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1tlp
catalytic residue: TYR 157;HIS 231
cofactor binding residue: GLU 166(Zinc binding)

1tlxA02
type: Pdb
references: 1tlx
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1tlx
catalytic residue: TYR 157;HIS 231
cofactor binding residue: GLU 166(Zinc binding)

1tmnE02
type: Pdb
references: 1tmn
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1tmn
catalytic residue: TYR 157;HIS 231
cofactor binding residue: GLU 166(Zinc binding)

2tliA02
type: Pdb
references: 2tli
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2tli
catalytic residue: TYR 157;HIS 231
cofactor binding residue: GLU 166(Zinc binding)

2tlxA02
type: Pdb
references: 2tlx
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2tlx
catalytic residue: TYR 157;HIS 231
cofactor binding residue: GLU 166(Zinc binding)

2tmnE02
type: Pdb
references: 2tmn
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2tmn
catalytic residue: TYR 157;HIS 231
cofactor binding residue: GLU 166(Zinc binding)

3tliA02
type: Pdb
references: 3tli
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3tli
catalytic residue: TYR 157;HIS 231
cofactor binding residue: GLU 166(Zinc binding)

3tlnA02
type: Pdb
references: 3tln
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3tln
catalytic residue: TYR 157;HIS 231
cofactor binding residue: GLU 166(Zinc binding)

3tmnE02
type: Pdb
references: 3tmn
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3tmn
catalytic residue: TYR 157;HIS 231
cofactor binding residue: GLU 166(Zinc binding)

4tliA02
type: Pdb
references: 4tli
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:4tli
catalytic residue: TYR 157;HIS 231
cofactor binding residue: GLU 166(Zinc binding)

4tlnA02
type: Pdb
references: 4tln
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:4tln
catalytic residue: TYR 157;HIS 231
cofactor binding residue: GLU 166(Zinc binding)

4tmnE02
type: Pdb
references: 4tmn
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:4tmn
catalytic residue: TYR 157;HIS 231
cofactor binding residue: GLU 166(Zinc binding)

5tliA02
type: Pdb
references: 5tli
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:5tli
catalytic residue: TYR 157;HIS 231
cofactor binding residue: GLU 166(Zinc binding)

5tlnA02
type: Pdb
references: 5tln
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:5tln
catalytic residue: TYR 157;HIS 231
cofactor binding residue: GLU 166(Zinc binding)

5tmnE02
type: Pdb
references: 5tmn
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:5tmn
catalytic residue: TYR 157;HIS 231
cofactor binding residue: GLU 166(Zinc binding)

6tliA02
type: Pdb
references: 6tli
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:6tli
catalytic residue: TYR 157;HIS 231
cofactor binding residue: GLU 166(Zinc binding)

6tmnE02
type: Pdb
references: 6tmn
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:6tmn
catalytic residue: TYR 157;HIS 231
cofactor binding residue: GLU 166(Zinc binding)

7tliA02
type: Pdb
references: 7tli
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:7tli
catalytic residue: TYR 157;HIS 231
cofactor binding residue: GLU 166(Zinc binding)

7tlnA02
type: Pdb
references: 7tln
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:7tln
catalytic residue: TYR 157;HIS 231
cofactor binding residue: GLU 166(Zinc binding)

8tliA02
type: Pdb
references: 8tli
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:8tli
catalytic residue: TYR 157;HIS 231
cofactor binding residue: GLU 166(Zinc binding)

8tlnE02
type: Pdb
references: 8tln
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:8tln
catalytic residue: TYR 157;HIS 231
cofactor binding residue: GLU 166(Zinc binding)

Analogue
compound: Peptide
pdb: 1qf2A01
ligand het code: TI3

Analogue
compound: Zinc
pdb: 1lnaE01
ligand het code: _CO_900

Analogue
compound: Zinc
pdb: 1lnbE01
ligand het code: _FE

Analogue
compound: Zinc
pdb: 1lncE01
ligand het code: _MN_900

Analogue
compound: Zinc
pdb: 1lneE01
ligand het code: _CD_900

TransitionStateAnalogue
pdb: 1hytA01
ligand het code: BZS

TransitionStateAnalogue
pdb: 1kjoA01
ligand het code: PHQ-THR

TransitionStateAnalogue
pdb: 1kjpA01
ligand het code: PHQ-GLU

TransitionStateAnalogue
pdb: 1kkkA01
ligand het code: PHQ-ASP

TransitionStateAnalogue
pdb: 1kl6A01
ligand het code: PHQ-ALA

TransitionStateAnalogue
pdb: 1kr6A01
ligand het code: PHQ-DGL

TransitionStateAnalogue
pdb: 1kroA01
ligand het code: PHQ-DTH

TransitionStateAnalogue
pdb: 1ks7A01
ligand het code: PHQ-DAS

TransitionStateAnalogue
pdb: 1ktoA01
ligand het code: PHQ-DAL

TransitionStateAnalogue
pdb: 1os0A01
ligand het code: PPH-DPH-PHE

TransitionStateAnalogue
pdb: 1qf0A01
ligand het code: TI2

TransitionStateAnalogue
pdb: 1qf1A01
ligand het code: TI1

TransitionStateAnalogue
pdb: 1thlA01
ligand het code: CLT-CCM-TRP

TransitionStateAnalogue
pdb: 1tlpE01
ligand het code: RHA-LEU-TRP

TransitionStateAnalogue
pdb: 1tmnE01
ligand het code: CLT-LEU-TRP

TransitionStateAnalogue
pdb: 2tmnE01
ligand het code: PO3-LEU-NH2

TransitionStateAnalogue
pdb: 4tlnA01
ligand het code: LNO

TransitionStateAnalogue
pdb: 4tmnE01
ligand het code: PHQ-PPH-LEU-ALA

TransitionStateAnalogue
pdb: 5tlnA01
ligand het code: BAN

TransitionStateAnalogue
pdb: 5tmnE01
ligand het code: PHQ-PGL-LEU-LEU

IntermediateAnalogue
pdb: 6tmnE01
ligand het code: PHQ-PGL-1LU-LEU

IntermediateAnalogue
pdb: 7tlnA01
ligand het code: INC

ReferenceForCatalyticMechanism
reference index: 3
reference section: Fig.5, p.6917-6920

ReferenceForCatalyticMechanism
reference index: 5

ReferenceForCatalyticMechanism
reference index: 6
reference section: p.5727-5728

ReferenceForCatalyticMechanism
reference index: 7

ReferenceForCatalyticMechanism
reference index: 8
reference section: Fig.1, p.8547-8549

ReferenceForCatalyticMechanism
reference index: 9

ReferenceForCatalyticMechanism
reference index: 10
reference section: p.3259

ReferenceForCatalyticMechanism
reference index: 17
reference section: Fig.1, p.16807-16808

ReferenceForCatalyticMechanism
reference index: 20
reference section: Scheme 1, p.7373

ReferenceForCatalyticMechanism
reference index: 42
reference section: Fig.2, Fig.3, p.287-296

Evidence of an essential histidine residue in thermolysin
type: BibliographicResource
comment: ACTIVE SITE.
medline id: 74052951
references: http://www.ncbi.nlm.nih.gov/pubmed/4808703
journal: Biochemistry
volume: 13
pages: 205-10
published year: 1974
authors:
  item: Burstein Y
  item: Walsh KA
  item: Neurath H
references: P00800

The conformation of thermolysin
type: BibliographicResource
comment: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
medline id: 75041142
references: http://www.ncbi.nlm.nih.gov/pubmed/4214815
journal: J Biol Chem
volume: 249
pages: 8030-44
published year: 1974
authors:
  item: Matthews BW
  item: Weaver LH
  item: Kester WR
references: P00800

Binding of hydroxamic acid inhibitors to crystalline thermolysin suggests a pentacoordinate zinc intermediate in catalysis
type: BibliographicResource
comment: X-ray crystallography
references: http://www.ncbi.nlm.nih.gov/pubmed/7317361
journal: Biochemistry
volume: 20
pages: 6912-20
published year: 1981
authors:
  item: Holmes MA
  item: Matthews BW
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl

Structure of thermolysin refined at 1.6 A resolution
type: BibliographicResource
comment: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS).
medline id: 83085812
references: http://www.ncbi.nlm.nih.gov/pubmed/7175940
journal: J Mol Biol
volume: 160
pages: 623-39
published year: 1982
authors:
  item: Holmes MA
  item: Matthews BW
references: P00800

Structural analysis of the inhibition of thermolysin by an active-site-directed irreversible inhibitor
type: BibliographicResource
comment: X-ray crystallography
references: http://www.ncbi.nlm.nih.gov/pubmed/6830761
journal: Biochemistry
volume: 22
pages: 236-40
published year: 1983
authors:
  item: Holmes MA
  item: Tronrud DE
  item: Matthews BW
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl

Binding of N-carboxymethyl dipeptide inhibitors to thermolysin determined by X-ray crystallography: a novel class of transition-state analogues for zinc peptidases
type: BibliographicResource
comment: X-ray crystallography
references: http://www.ncbi.nlm.nih.gov/pubmed/6395881
journal: Biochemistry
volume: 23
pages: 5724-9
published year: 1984
authors:
  item: Monzingo AF
  item: Matthews BW
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl

Crystallographic structural analysis of phosphoramidates as inhibitors and transition-state analogs of thermolysin
type: BibliographicResource
comment: X-ray crystallography
references: http://www.ncbi.nlm.nih.gov/pubmed/3709536
journal: Eur J Biochem
volume: 157
pages: 261-8
published year: 1986
authors:
  item: Tronrud DE
  item: Monzingo AF
  item: Matthews BW
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl

Slow- and fast-binding inhibitors of thermolysin display different modes of binding: crystallographic analysis of extended phosphonamidate transition-state analogues
type: BibliographicResource
comment: X-ray crystallography
references: http://www.ncbi.nlm.nih.gov/pubmed/3442675
journal: Biochemistry
volume: 26
pages: 8542-53
published year: 1987
authors:
  item: Holden HM
  item: Tronrud DE
  item: Monzingo AF
  item: Weaver LH
  item: Matthews BW
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl

Structures of two thermolysin-inhibitor complexes that differ by a single hydrogen bond
type: BibliographicResource
comment: X-ray crystallography
references: http://www.ncbi.nlm.nih.gov/pubmed/3810156
journal: Science
volume: 235
pages: 571-4
published year: 1987
authors:
  item: Tronrud DE
  item: Holden HM
  item: Matthews BW
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl

The binding of L-valyl-L-tryptophan to crystalline thermolysin illustrates the mode of interaction of a product of peptide hydrolysis
type: BibliographicResource
comment: X-ray crystallography
references: http://www.ncbi.nlm.nih.gov/pubmed/3343246
journal: J Biol Chem
volume: 263
pages: 3256-60
published year: 1988
authors:
  item: Holden HM
  item: Matthews BW
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl

Thermolysin as a catalyst in enzymatic synthesis of asparagine-containing peptides II
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/2019475
journal: Int J Pept Protein Res
volume: 37
pages: 128-33
published year: 1991
authors:
  item: Miranda MT
  item: Tominaga M

Structural comparison suggests that thermolysin and related neutral proteases undergo hinge-bending motion during catalysis
type: BibliographicResource
comment: X-ray crystallography
references: http://www.ncbi.nlm.nih.gov/pubmed/1445869
journal: Biochemistry
volume: 31
pages: 11310-6
published year: 1992
authors:
  item: Holland DR
  item: Tronrud DE
  item: Pley HW
  item: Flaherty KM
  item: Stark W
  item: Jansonius JN
  item: McKay DB
  item: Matthews BW
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl

Inhibition of thermolysin and neutral endopeptidase 24.11 by a novel glutaramide derivative: X-ray structure determination of the thermolysin-inhibitor complex
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/8286362
journal: Biochemistry
volume: 33
pages: 51-6
published year: 1994
authors:
  item: Holland DR
  item: Barclay PL
  item: Danilewicz JC
  item: Matthews BW
  item: James K
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl

NMR solution structure of the C-terminal fragment 255-316 of thermolysin: a dimer formed by subunits having the native structure
type: BibliographicResource
comment: STRUCTURE BY NMR OF 487-548.
medline id: 95086079
references: http://www.ncbi.nlm.nih.gov/pubmed/7993910
journal: Biochemistry
volume: 33
pages: 14834-47
published year: 1994
authors:
  item: Rico M
  item: Jimenez MA
  item: Gonzalez C
  item: De Filippis V
  item: Fontana A
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P00800

Redetermination and refinement of the complex of benzylsuccinic acid with thermolysin and its relation to the complex with carboxypeptidase A
type: BibliographicResource
comment: X-ray crystallography
references: http://www.ncbi.nlm.nih.gov/pubmed/8034637
journal: J Biol Chem
volume: 269
pages: 18839-42
published year: 1994
authors:
  item: Hausrath AC
  item: Matthews BW
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl

Observation of the pre-steady state process in thermolysin catalysis with a fluorescent displacement probe at low pH
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/7720870
journal: FEBS Lett
volume: 362
pages: 189-91
published year: 1995
authors:
  item: Kunugi S
  item: Yokoyama M
  item: Sakamoto A

The role of histidine 231 in thermolysin-like enzymes. A site-directed mutagenesis study
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/7622493
journal: J Biol Chem
volume: 270
pages: 16803-8
published year: 1995
authors:
  item: Beaumont A
  item: O'Donohue MJ
  item: Paredes N
  item: Rousselet N
  item: Assicot M
  item: Bohuon C
  item: Fournie-Zaluski MC
  item: Roques BP

Solid-state nuclear magnetic resonance analysis of the conformation of an inhibitor bound to thermolysin
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/7629812
journal: J Med Chem
volume: 38
pages: 2742-7
published year: 1995
authors:
  item: Beusen DD
  item: McDowell LM
  item: Slomczynska U
  item: Schaefer J

Structural analysis of zinc substitutions in the active site of thermolysin
type: BibliographicResource
comment: X-ray crystallography
references: http://www.ncbi.nlm.nih.gov/pubmed/8535232
journal: Protein Sci
volume: 4
pages: 1955-65
published year: 1995
authors:
  item: Holland DR
  item: Hausrath AC
  item: Juers D
  item: Matthews BW
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl

Arazoformyl dipeptide substrates for thermolysin. Confirmation of a reverse protonation catalytic mechanism
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/8652513
journal: Biochemistry
volume: 35
pages: 7369-77
published year: 1996
authors:
  item: Mock WL
  item: Stanford DJ

NMR solution structure of the 205-316 C-terminal fragment of thermolysin. An example of dimerization coupled to partial unfolding
type: BibliographicResource
comment: STRUCTURE BY NMR OF 437-548.
medline id: 97452621
references: http://www.ncbi.nlm.nih.gov/pubmed/9305992
journal: Biochemistry
volume: 36
pages: 11975-83
published year: 1997
authors:
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Synthesis of dipeptides by suspension-to-suspension conversion via thermolysin catalysis: from analytical to preparative scale
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Model building of a thermolysin-like protease by mutagenesis.
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Enzymatic and structural approaches of the thermolysin mechanism in glycerol-containing media
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Testing for diffusion limitations in salt-activated enzyme catalysts operating in organic solvents
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Intramolecular processing of prothermolysin
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Elucidation of the mode of interaction of thermolysin with a proteinaceous metalloproteinase inhibitor, SMPI, based on a model complex structure and a structural dynamics analysis
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Crystal structures of alpha-mercaptoacyldipeptides in the thermolysin active site: structural parameters for a Zn monodentation or bidentation in metalloendopeptidases
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comment: X-ray crystallography
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Characterization of a novel stable biocatalyst obtained by protein engineering.
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Locating interaction sites on proteins: the crystal structure of thermolysin soaked in 2% to 100% isopropanol
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comment: X-ray crystallography
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Substrate specificity in the highly heterogeneous M4 peptidase family is determined by a small subset of amino acids.
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A novel method of aligning molecules by local surface shape similarity
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An evolutionary computational approach to the phase problem in macromolecular X-ray crystallography
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Novel kinetic analysis of enzymatic dipeptide synthesis: effect of pH and substrates on thermolysin catalysis
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Experimental and computational mapping of the binding surface of a crystalline protein
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comment: X-ray crystallography
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The 2.2 A resolution structure of thermolysin (TLN) crystallized in the presence of potassium thiocyanate.
type: BibliographicResource
comment: X-ray crystallography
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Thermolysin in the absence of substrate has an open conformation
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comment: X-ray crystallography
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journal: Acta Crystallogr D Biol Crystallogr
volume: 58
pages: 1002-7
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Efficient transesterification of sucrose catalysed by the metalloprotease thermolysin in dimethylsulfoxide
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journal: FEBS Lett
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Molecular imprinting of enzymes with water-insoluble ligands for nonaqueous biocatalysis
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journal: J Am Chem Soc
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The effects of modifying the surface charge on the catalytic activity of a thermolysin-like protease.
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A theoretical study of the mechanism for peptide hydrolysis by thermolysin.
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journal: J Biol Inorg Chem
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pages: 284-98
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Consensus scoring for ligand/protein interactions
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Interactions of a new alpha-aminophosphinic derivative inside the active site of TLN (thermolysin): a model for zinc-metalloendopeptidase inhibition.
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comment: X-ray crystallography
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A cyclic metallopeptide induces alpha helicity in short peptide fragments of thermolysin.
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Origin of the stereospecificity in binding hydroxamates of alpha- and beta-phenylalanine methylamide to thermolysin revealed by the X-ray crystallographic study.
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Bacillus thermoproteolyticus neutral proteinase
type: KeggEnzyme

thermoase
type: KeggEnzyme

thermoase Y10
type: KeggEnzyme

TLN
type: KeggEnzyme