DB code: S00398

RLCP classification 1.13.11400.460 : Hydrolysis
CATH domain 3.40.390.10 : Collagenase (Catalytic Domain) Catalytic domain
E.C. 3.4.24.42
CSA
M-CSA
MACiE

CATH domain Related DB codes (homologues)
3.40.390.10 : Collagenase (Catalytic Domain) S00394 S00395 S00397 S00399 D00232 D00236 M00101

Uniprot Enzyme Name
UniprotKB Protein name Synonyms MEROPS Pfam
P15167 Zinc metalloproteinase atrolysin-D
EC 3.4.24.42
Hemorrhagic metalloproteinase atrolysin D
Hemorrhagic toxin D
HT-D
M12.144 (Metallo)
PF01562 (Pep_M12B_propep)
PF01421 (Reprolysin)
[Graphical View]

KEGG enzyme name
atrolysin C
Crotalus atrox metalloendopeptidase c
hemorrhagic toxin c and d

UniprotKB: Accession Number Entry name Activity Subunit Subcellular location Cofactor
P15167 VMATD_CROAT Cleavage of 5-His-|-Leu-6, 10-His-|-Leu-11, 14-Ala-|-Leu-15, 16-Tyr-|-Leu-17 and 23-Gly-|-Phe-24 of insulin B chain. With small molecule substrates prefers hydrophobic residue at P2'' and small residue such as Ala, Gly at P1. Secreted. Binds 1 calcium ion per subunit. Binds 1 zinc ion per subunit.

KEGG Pathways
Map code Pathways E.C.

Compound table
Cofactors Substrates Products Intermediates
KEGG-id C00038 C00017 C00012 C00001 C00017 C00012
E.C.
Compound Zinc Protein Peptide H2O Protein Peptide
Type heavy metal peptide/protein peptide/protein H2O peptide/protein peptide/protein
ChEBI 29105
 29105
 		15377
 15377
PubChem 32051
 32051
 		22247451
 962
 22247451
 962
1atlA Bound:_ZN Unbound Unbound Unbound Unbound
1atlB Bound:_ZN Unbound Unbound Unbound Unbound
1dthA Bound:_ZN Unbound Unbound Unbound Unbound
1dthB Bound:_ZN Unbound Unbound Unbound Unbound
1htdA Bound:_ZN Unbound Unbound Unbound Unbound
1htdB Bound:_ZN Unbound Unbound Unbound Unbound

Reference for Active-site residues
resource references E.C.

Active-site residues
PDB Catalytic residues Cofactor-binding residues Modified residues Main-chain involved in catalysis Comment
1atlA GLU 143 HIS 142;HIS 146;HIS 152(Zinc binding)
1atlB GLU 143 HIS 142;HIS 146;HIS 152(Zinc binding)
1dthA GLU 143 HIS 142;HIS 146;HIS 152(Zinc binding)
1dthB GLU 143 HIS 142;HIS 146;HIS 152(Zinc binding)
1htdA GLU 143 HIS 142;HIS 146;HIS 152(Zinc binding)
1htdB GLU 143 HIS 142;HIS 146;HIS 152(Zinc binding)

References for Catalytic Mechanism
References Sections No. of steps in catalysis
[1]

References
[1]
Resource
Comments X-ray crystallography
Medline ID 94359948
PubMed ID 8078901
Journal Proc Natl Acad Sci U S A
Year 1994
Volume 91
Pages 8447-51
Authors Zhang D, Botos I, Gomis-Ruth FX, Doll R, Blood C, Njoroge FG, Fox JW, Bode W, Meyer EF
Title Structural interaction of natural and synthetic inhibitors with the venom metalloproteinase, atrolysin C (form d).
Related PDB 1atl 1htd
Related UniProtKB P15167
[2]
Resource
Comments X-ray crystallography (2.0 Angstroms)
Medline ID
PubMed ID 8610113
Journal Proc Natl Acad Sci U S A
Year 1996
Volume 93
Pages 2749-54
Authors Botos I, Scapozza L, Zhang D, Liotta LA, Meyer EF
Title Batimastat, a potent matrix mealloproteinase inhibitor, exhibits an unexpected mode of binding.
Related PDB 1dth
Related UniProtKB
[3]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 12071970
Journal Eur J Biochem
Year 2002
Volume 269
Pages 3047-56
Authors Huang KF, Chiou SH, Ko TP, Wang AH
Title Determinants of the inhibition of a Taiwan habu venom metalloproteinase by its endogenous inhibitors revealed by X-ray crystallography and synthetic inhibitor analogues.
Related PDB
Related UniProtKB

Comments
This enzyme belongs to the peptidase family-M12B.
The zinc ion is catalytic in this enzyme (see [1]).

Created Updated
2002-09-12 2009-02-26