T00095
type: Enzyme
cath: Fumarase C; Chain B, domain 1
cath: Fumarase C; Chain A, domain 2
cath: Ribonucleotide Reductase Protein R1; domain 1
ec: https://purl.uniprot.org/enzyme/4.3.2.2
csa: 1c3c
macie: M0080
uniprot: Q8ZY28
uniprot: Q9X0I0
kegg enzyme: adenylosuccinate lyase
kegg enzyme: adenylosuccinase
kegg enzyme: succino AMP-lyase
kegg enzyme: 6-N-(1,2-dicarboxyethyl)AMP AMP-lyase
kegg enzyme: 6-N-(1,2-dicarboxyethyl)AMP AMP-lyase (fumarate-forming)
kegg pathway: Purine metabolism
kegg pathway: Alanine and aspartate metabolism
kegg substrate: N6-(1,2-Dicarboxyethyl)-AMP
kegg substrate: 1-(5'-Phosphoribosyl)-4-(N-succinocarboxamide)-5-aminoimidazole
kegg product: Fumarate
kegg product: AMP
kegg product: 1-(5'-Phosphoribosyl)-5-amino-4-imidazolecarboxamide
pdb: 1dofA01
pdb: 1dofB01
pdb: 1dofC01
pdb: 1dofD01
pdb: 1c3cA01
pdb: 1c3cB01
pdb: 1c3uA01
pdb: 1c3uB01
pdb: 1dofA02
pdb: 1dofB02
pdb: 1dofC02
pdb: 1dofD02
pdb: 1c3cA02
pdb: 1c3cB02
pdb: 1c3uA02
pdb: 1c3uB02
pdb: 1dofA03
pdb: 1dofB03
pdb: 1dofC03
pdb: 1dofD03
pdb: 1c3cA03
pdb: 1c3cB03
pdb: 1c3uA03
pdb: 1c3uB03
pdb bound state: Unbound
  compound: N6-(1,2-Dicarboxyethyl)-AMP
  pdb: 1dofA01
pdb bound state: Unbound
  compound: N6-(1,2-Dicarboxyethyl)-AMP
  pdb: 1dofB01
pdb bound state: Unbound
  compound: N6-(1,2-Dicarboxyethyl)-AMP
  pdb: 1dofC01
pdb bound state: Unbound
  compound: N6-(1,2-Dicarboxyethyl)-AMP
  pdb: 1dofD01
pdb bound state: Unbound
  compound: N6-(1,2-Dicarboxyethyl)-AMP
  pdb: 1c3cA01
pdb bound state: Unbound
  compound: N6-(1,2-Dicarboxyethyl)-AMP
  pdb: 1c3cB01
pdb bound state: Unbound
  compound: N6-(1,2-Dicarboxyethyl)-AMP
  pdb: 1c3uA01
pdb bound state: Unbound
  compound: N6-(1,2-Dicarboxyethyl)-AMP
  pdb: 1c3uB01
pdb bound state: Unbound
  compound: N6-(1,2-Dicarboxyethyl)-AMP
  pdb: 1dofA02
pdb bound state: Unbound
  compound: N6-(1,2-Dicarboxyethyl)-AMP
  pdb: 1dofB02
pdb bound state: Unbound
  compound: N6-(1,2-Dicarboxyethyl)-AMP
  pdb: 1dofC02
pdb bound state: Unbound
  compound: N6-(1,2-Dicarboxyethyl)-AMP
  pdb: 1dofD02
pdb bound state: Unbound
  compound: N6-(1,2-Dicarboxyethyl)-AMP
  pdb: 1c3cA02
pdb bound state: Unbound
  compound: N6-(1,2-Dicarboxyethyl)-AMP
  pdb: 1c3cB02
pdb bound state: Unbound
  compound: N6-(1,2-Dicarboxyethyl)-AMP
  pdb: 1c3uA02
pdb bound state: Unbound
  compound: N6-(1,2-Dicarboxyethyl)-AMP
  pdb: 1c3uB02
pdb bound state: Unbound
  compound: N6-(1,2-Dicarboxyethyl)-AMP
  pdb: 1dofA03
pdb bound state: Unbound
  compound: N6-(1,2-Dicarboxyethyl)-AMP
  pdb: 1dofB03
pdb bound state: Unbound
  compound: N6-(1,2-Dicarboxyethyl)-AMP
  pdb: 1dofC03
pdb bound state: Unbound
  compound: N6-(1,2-Dicarboxyethyl)-AMP
  pdb: 1dofD03
pdb bound state: Unbound
  compound: N6-(1,2-Dicarboxyethyl)-AMP
  pdb: 1c3cA03
pdb bound state: Unbound
  compound: N6-(1,2-Dicarboxyethyl)-AMP
  pdb: 1c3cB03
active site residues resources: A key role in catalysis for His89 of adenylosuccinate lyase of Bacillus subtilis.
active site residues resources: http://ezcatdb.cbrc.jp/EzCatDB/reference/T00095#10
active site residues resources: Q9X0I0
references: Metabolism of threo-beta-fluoroaspartate by H4 cells. Inhibition of adenylosuccinate lyase by fluoro analogs of its substrates.
references: The multisubunit active site of fumarase C from Escherichia coli.
references: The purB gene of Escherichia coli K-12 is located in an operon.
references: Crystallization and preliminary structural analysis of Bacillus subtilis adenylosuccinate lyase, an enzyme implicated in infantile autism.
references: His68 and His141 are critical contributors to the intersubunit catalytic site of adenylosuccinate lyase of Bacillus subtilis.
references: A key role in catalysis for His89 of adenylosuccinate lyase of Bacillus subtilis.
references: The crystal structure of adenylosuccinate lyase from Pyrobaculum aerophilum reveals an intracellular protein with three disulfide bonds.
references: The structure of adenylosuccinate lyase, an enzyme with dual activity in the de novo purine biosynthetic pathway.
references: Three subunits contribute amino acids to the active site of tetrameric adenylosuccinate lyase: Lys268 and Glu275 are required.
comment: This enzyme catalyzes two similar reactions, in which fumarate will be cut from nucleotide derivatives. The active site and catalytic mechanism seem to be shared by these reactions.

Fumarase C; Chain B, domain 1
type: Cath
references: http://www.cathdb.info/version/latest/superfamily/1.10.275.10
catalytic domain: index.html

Fumarase C; Chain A, domain 2
type: Cath
references: http://www.cathdb.info/version/latest/superfamily/1.20.200.10
catalytic domain: index.html

Ribonucleotide Reductase Protein R1; domain 1
type: Cath
references: http://www.cathdb.info/version/latest/superfamily/1.10.40.30

Purine metabolism
type: KeggPathway
references: KEGG:MAP00230

Alanine and aspartate metabolism
type: KeggPathway
references: KEGG:MAP00252

N6-(1,2-Dicarboxyethyl)-AMP
type: KeggSubstrate
references: KEGG:C03794
compound type: amino acids
compound type: carboxyl group
compound type: nucleotide
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

1-(5'-Phosphoribosyl)-4-(N-succinocarboxamide)-5-aminoimidazole
type: KeggSubstrate
references: KEGG:C04823
compound type: amino acids
compound type: amide group
compound type: amine group
compound type: carbohydrate
compound type: nucleotide
references: CHEBI:18319
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

Fumarate
type: KeggProduct
references: KEGG:C00122
compound type: carboxyl group
references: CHEBI:18012
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

AMP
type: KeggProduct
references: KEGG:C00020
compound type: amine group
compound type: nucleotide
references: CHEBI:16027
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

1-(5'-Phosphoribosyl)-5-amino-4-imidazolecarboxamide
type: KeggProduct
references: KEGG:C04677
compound type: amide group
compound type: amine group
compound type: nucleotide
references: CHEBI:18406
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

1dofA01
type: Pdb
references: 1dof
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1dof
catalytic residue: HIS 72
comment: invisible 64-71

1dofB01
type: Pdb
references: 1dof
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1dof
catalytic residue: HIS 72
comment: invisible 64-71

1dofC01
type: Pdb
references: 1dof
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1dof
catalytic residue: HIS 72
comment: invisible 64-71

1dofD01
type: Pdb
references: 1dof
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1dof
catalytic residue: HIS 72
comment: invisible 64-71

1c3cA01
type: Pdb
references: 1c3c
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1c3c
catalytic residue: HIS 68

1c3cB01
type: Pdb
references: 1c3c
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1c3c
catalytic residue: HIS 68

1c3uA01
type: Pdb
references: 1c3u
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1c3u
catalytic residue: HIS 68

1c3uB01
type: Pdb
references: 1c3u
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1c3u
catalytic residue: HIS 68

1dofA02
type: Pdb
references: 1dof
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1dof
catalytic residue: HIS 143;GLU 275
comment: invisible 260-268

1dofB02
type: Pdb
references: 1dof
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1dof
catalytic residue: HIS 143;GLU 275
comment: invisible 260-268

1dofC02
type: Pdb
references: 1dof
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1dof
catalytic residue: HIS 143;GLU 275
comment: invisible 260-268

1dofD02
type: Pdb
references: 1dof
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1dof
catalytic residue: HIS 143;GLU 275
comment: invisible 260-268

1c3cA02
type: Pdb
references: 1c3c
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1c3c
catalytic residue: HIS 141;GLU 275

1c3cB02
type: Pdb
references: 1c3c
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1c3c
catalytic residue: HIS 141;GLU 275

1c3uA02
type: Pdb
references: 1c3u
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1c3u
catalytic residue: HIS 141;GLU 275

1c3uB02
type: Pdb
references: 1c3u
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1c3u
catalytic residue: HIS 141;GLU 275

Metabolism of threo-beta-fluoroaspartate by H4 cells. Inhibition of adenylosuccinate lyase by fluoro analogs of its substrates.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/3759987
journal: J Biol Chem
volume: 261
pages: 13637-42
published year: 1986
authors:
  item: Casey PJ
  item: Abeles RH
  item: Lowenstein JM

The multisubunit active site of fumarase C from Escherichia coli.
type: BibliographicResource
comment: Homologous enzymes
references: http://www.ncbi.nlm.nih.gov/pubmed/7552727
journal: Nat Struct Biol
volume: 2
pages: 654-62
published year: 1995
authors:
  item: Weaver TM
  item: Levitt DG
  item: Donnelly MI
  item: Stevens PP
  item: Banaszak LJ

The purB gene of Escherichia coli K-12 is located in an operon.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/8969519
journal: Microbiology
volume: 142
pages: 3219-30
published year: 1996
authors:
  item: Green SM
  item: Malik T
  item: Giles IG
  item: Drabble WT

Crystallization and preliminary structural analysis of Bacillus subtilis adenylosuccinate lyase, an enzyme implicated in infantile autism.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/8845770
journal: Protein Sci
volume: 5
pages: 786-8
published year: 1996
authors:
  item: Redinbo MR
  item: Eide SM
  item: Stone RL
  item: Dixon JE
  item: Yeates TO

His68 and His141 are critical contributors to the intersubunit catalytic site of adenylosuccinate lyase of Bacillus subtilis.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/9890879
journal: Biochemistry
volume: 38
pages: 22-32
published year: 1999
authors:
  item: Lee TT
  item: Worby C
  item: Bao ZQ
  item: Dixon JE
  item: Colman RF

A key role in catalysis for His89 of adenylosuccinate lyase of Bacillus subtilis.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/11063569
journal: Biochemistry
volume: 39
pages: 13336-43
published year: 2000
authors:
  item: Brosius JL
  item: Colman RF

The crystal structure of adenylosuccinate lyase from Pyrobaculum aerophilum reveals an intracellular protein with three disulfide bonds.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/10926519
journal: J Mol Biol
volume: 301
pages: 433-50
published year: 2000
authors:
  item: Toth EA
  item: Worby C
  item: Dixon JE
  item: Goedken ER
  item: Marqusee S
  item: Yeates TO
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl

The structure of adenylosuccinate lyase, an enzyme with dual activity in the de novo purine biosynthetic pathway.
type: BibliographicResource
comment: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
medline id: 20139703
references: http://www.ncbi.nlm.nih.gov/pubmed/10673438
journal: Structure Fold Des
volume: 8
pages: 163-74
published year: 2000
authors:
  item: Toth EA
  item: Yeates TO
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: Q9X0I0

Three subunits contribute amino acids to the active site of tetrameric adenylosuccinate lyase: Lys268 and Glu275 are required.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/11841213
journal: Biochemistry
volume: 41
pages: 2217-26
published year: 2002
authors:
  item: Brosius JL
  item: Colman RF

ReferenceForCatalyticMechanism
reference index: 2
reference section: Fig.1, p.660-661

ReferenceForCatalyticMechanism
reference index: 8
reference section: Fig.5c, p.166-169
reference step: 2

ReferenceForCatalyticMechanism
reference index: 9
reference section: p.2224