T00092
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/4.3.1.1
uniprot: P0AC38
kegg enzyme: aspartate ammonia-lyase
kegg enzyme: aspartase
kegg enzyme: fumaric aminase
kegg enzyme: L-aspartase
kegg enzyme: L-aspartate ammonia-lyase
kegg pathway: Alanine and aspartate metabolism
kegg pathway: Nitrogen metabolism
kegg substrate: L-Aspartate
kegg product: Fumarate
kegg product: NH3
pdb: 1jswA01
pdb: 1jswB01
pdb: 1jswC01
pdb: 1jswD01
pdb: 1jswA02
pdb: 1jswB02
pdb: 1jswC02
pdb: 1jswD02
pdb: 1jswA03
pdb: 1jswB03
pdb: 1jswD03
pdb bound state: Unbound
  compound: L-Aspartate
  pdb: 1jswA01
pdb bound state: Unbound
  compound: L-Aspartate
  pdb: 1jswB01
pdb bound state: Unbound
  compound: L-Aspartate
  pdb: 1jswC01
pdb bound state: Unbound
  compound: L-Aspartate
  pdb: 1jswD01
pdb bound state: Unbound
  compound: L-Aspartate
  pdb: 1jswA02
pdb bound state: Unbound
  compound: L-Aspartate
  pdb: 1jswB02
pdb bound state: Unbound
  compound: L-Aspartate
  pdb: 1jswC02
pdb bound state: Unbound
  compound: L-Aspartate
  pdb: 1jswD02
pdb bound state: Unbound
  compound: L-Aspartate
  pdb: 1jswA03
pdb bound state: Unbound
  compound: L-Aspartate
  pdb: 1jswB03
pdb bound state: Unbound
  compound: L-Aspartate
  pdb: 1jswD03
pdb bound state: Unbound
  compound: Fumarate
  pdb: 1jswA01
pdb bound state: Unbound
  compound: Fumarate
  pdb: 1jswB01
pdb bound state: Unbound
  compound: Fumarate
  pdb: 1jswC01
pdb bound state: Unbound
  compound: Fumarate
  pdb: 1jswD01
pdb bound state: Unbound
  compound: Fumarate
  pdb: 1jswA02
pdb bound state: Unbound
  compound: Fumarate
  pdb: 1jswB02
pdb bound state: Unbound
  compound: Fumarate
  pdb: 1jswC02
pdb bound state: Unbound
  compound: Fumarate
  pdb: 1jswD02
pdb bound state: Unbound
  compound: Fumarate
  pdb: 1jswA03
pdb bound state: Unbound
  compound: Fumarate
  pdb: 1jswB03
pdb bound state: Unbound
  compound: Fumarate
  pdb: 1jswD03
pdb bound state: Unbound
  compound: NH3
  pdb: 1jswA01
pdb bound state: Unbound
  compound: NH3
  pdb: 1jswB01
pdb bound state: Unbound
  compound: NH3
  pdb: 1jswC01
pdb bound state: Unbound
  compound: NH3
  pdb: 1jswD01
pdb bound state: Unbound
  compound: NH3
  pdb: 1jswA02
pdb bound state: Unbound
  compound: NH3
  pdb: 1jswB02
pdb bound state: Unbound
  compound: NH3
  pdb: 1jswC02
pdb bound state: Unbound
  compound: NH3
  pdb: 1jswD02
pdb bound state: Unbound
  compound: NH3
  pdb: 1jswA03
pdb bound state: Unbound
  compound: NH3
  pdb: 1jswB03
active site residues resources: Cloning and over-expression of thermostable Bacillus sp. YM55-1 aspartase and site-directed mutagenesis for probing a catalytic residue.
references: Studies on aspartase. II. Role of sulfhydryl groups in aspartase from Escherichia coli.
references: Studies on aspartase. V. Denaturant-mediated reactivation of aspartase, which has been otherwise irreversibly inactivated by various causes.
references: Acetylation-induced alteration of catalytic and regulatory properties of aspartase.
references: L-aspartase from Escherichia coli: substrate specificity and role of divalent metal ions.
references: Effect of detergents on aspartate ammonia-lyase activity in Escherichia alcalescens.
references: Activation of aspartase by site-directed mutagenesis.
references: Use of hybridization for distance measurement by fluorescence energy transfer in oligomeric proteins: distance between two functional sites in aspartase.
references: Cloning and nucleotide sequence of the Bacillus subtilis ansR gene, which encodes a repressor of the ans operon coding for L-asparaginase and L-aspartase.
references: Characterization of three types of aspartase activated by site-directed mutagenesis, limited proteolysis, and acetylation.
references: Crystallization and preliminary X-ray studies of L-aspartase from Escherichia coli.
references: Elimination of the sensitivity of L-aspartase to active-site-directed inactivation without alteration of catalytic activity.
references: The multisubunit active site of fumarase C from Escherichia coli.
references: The structure of L-aspartate ammonia-lyase from Escherichia coli.
references: Evaluation of functionally important amino acids in L-aspartate ammonia-lyase from Escherichia coli.
references: Studies on the properties of mutants of aspartase from Escherichia coli W.
references: Recovery of catalytic activity from an inactive aggregated mutant of l-aspartase.
references: L-aspartase: new tricks from an old enzyme.
references: Cloning and over-expression of thermostable Bacillus sp. YM55-1 aspartase and site-directed mutagenesis for probing a catalytic residue.
references: A monomeric L-aspartase obtained by in vitro selection.
comment: Although this enzyme requires a divalent metal ion per subunit, it is not involved in catalytic reaction, according to the literature [4]. It may contribute to the stability of the enzyme (see [17]).

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

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

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

Nitrogen metabolism
type: KeggPathway
references: KEGG:MAP00910

L-Aspartate
type: KeggSubstrate
references: KEGG:C00049
compound type: amino acids
compound type: carboxyl group
references: CHEBI:17053
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

NH3
type: KeggProduct
references: KEGG:C00014
compound type: amine group
compound type: organic ion
references: CHEBI:16134
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

1jswA02
type: Pdb
references: 1jsw
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1jsw
catalytic residue: SER 143

1jswB02
type: Pdb
references: 1jsw
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1jsw
catalytic residue: SER 143

1jswC02
type: Pdb
references: 1jsw
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1jsw
catalytic residue: SER 143

1jswD02
type: Pdb
references: 1jsw
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1jsw
catalytic residue: SER 143

Studies on aspartase. II. Role of sulfhydryl groups in aspartase from Escherichia coli.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/240429
journal: Biochim Biophys Acta
volume: 403
pages: 221-31
published year: 1975
authors:
  item: Mizuta K
  item: Tokushige M

Studies on aspartase. V. Denaturant-mediated reactivation of aspartase, which has been otherwise irreversibly inactivated by various causes.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/339956
journal: Biochim Biophys Acta
volume: 522
pages: 243-50
published year: 1978
authors:
  item: Tokushige M
  item: Eguchi G

Acetylation-induced alteration of catalytic and regulatory properties of aspartase.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/6357281
journal: Biochim Biophys Acta
volume: 749
pages: 101-5
published year: 1983
authors:
  item: Yumoto N
  item: Tokushige M

L-aspartase from Escherichia coli: substrate specificity and role of divalent metal ions.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/2853974
journal: Biochemistry
volume: 27
pages: 9089-93
published year: 1988
authors:
  item: Falzone CJ
  item: Karsten WE
  item: Conley JD
  item: Viola RE

Effect of detergents on aspartate ammonia-lyase activity in Escherichia alcalescens.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/3371801
journal: Folia Microbiol (Praha)
volume: 33
pages: 101-7
published year: 1988
authors:
  item: Malanik V
  item: Malanikova M
  item: Psenicka I
  item: Sojkova I
  item: Marek M

Activation of aspartase by site-directed mutagenesis.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/2043125
journal: Biochem Biophys Res Commun
volume: 177
pages: 414-9
published year: 1991
authors:
  item: Murase S
  item: Takagi JS
  item: Higashi Y
  item: Imaishi H
  item: Yumoto N
  item: Tokushige M

Use of hybridization for distance measurement by fluorescence energy transfer in oligomeric proteins: distance between two functional sites in aspartase.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/8216244
journal: Biochem Biophys Res Commun
volume: 195
pages: 1159-64
published year: 1993
authors:
  item: Murase S
  item: Kawata Y
  item: Yumoto N

Cloning and nucleotide sequence of the Bacillus subtilis ansR gene, which encodes a repressor of the ans operon coding for L-asparaginase and L-aspartase.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/8478318
journal: J Bacteriol
volume: 175
pages: 2501-6
published year: 1993
authors:
  item: Sun D
  item: Setlow P

Characterization of three types of aspartase activated by site-directed mutagenesis, limited proteolysis, and acetylation.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/8113229
journal: J Biochem (Tokyo)
volume: 114
pages: 735-9
published year: 1993
authors:
  item: Murase S
  item: Yumoto N

Crystallization and preliminary X-ray studies of L-aspartase from Escherichia coli.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/8263924
journal: J Mol Biol
volume: 234
pages: 1248-9
published year: 1993
authors:
  item: Shi W
  item: Kidd R
  item: Giorgianni F
  item: Schindler JF
  item: Viola RE
  item: Farber GK

Elimination of the sensitivity of L-aspartase to active-site-directed inactivation without alteration of catalytic activity.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/7893648
journal: Biochemistry
volume: 34
pages: 3529-35
published year: 1995
authors:
  item: Giorgianni F
  item: Beranova S
  item: Wesdemiotis C
  item: Viola RE

The multisubunit active site of fumarase C from Escherichia coli.
type: BibliographicResource
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 structure of L-aspartate ammonia-lyase from Escherichia coli.
type: BibliographicResource
comment: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS)
medline id: 97375637
references: http://www.ncbi.nlm.nih.gov/pubmed/9230045
journal: Biochemistry
volume: 36
pages: 9136-44
published year: 1997
authors:
  item: Shi W
  item: Dunbar J
  item: Jayasekera MM
  item: Viola RE
  item: Farber GK
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P0AC38

Evaluation of functionally important amino acids in L-aspartate ammonia-lyase from Escherichia coli.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/9230046
journal: Biochemistry
volume: 36
pages: 9145-50
published year: 1997
authors:
  item: Jayasekera MM
  item: Shi W
  item: Farber GK
  item: Viola RE

Studies on the properties of mutants of aspartase from Escherichia coli W.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/9928150
journal: Ann N Y Acad Sci
volume: 864
pages: 631-5
published year: 1998
authors:
  item: Lu J
  item: Zhang J
  item: Zhang H
  item: Wang X

Recovery of catalytic activity from an inactive aggregated mutant of l-aspartase.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/10529408
journal: Biochem Biophys Res Commun
volume: 264
pages: 596-600
published year: 1999
authors:
  item: Jayasekera MM
  item: Viola RE

L-aspartase: new tricks from an old enzyme.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/10800598
journal: Adv Enzymol Relat Areas Mol Biol
volume: 74
pages: 295-341
published year: 2000
authors:
  item: Viola RE

Cloning and over-expression of thermostable Bacillus sp. YM55-1 aspartase and site-directed mutagenesis for probing a catalytic residue.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/10712618
journal: Eur J Biochem
volume: 267
pages: 1847-57
published year: 2000
authors:
  item: Kawata Y
  item: Tamura K
  item: Kawamura M
  item: Ikei K
  item: Mizobata T
  item: Nagai J
  item: Fujita M
  item: Yano S
  item: Tokushige M
  item: Yumoto N

A monomeric L-aspartase obtained by in vitro selection.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/11983692
journal: J Biol Chem
volume: 277
pages: 24289-93
published year: 2002
authors:
  item: Kong X
  item: Li Z
  item: Gou X
  item: Zhu S
  item: Zhang H
  item: Wang X
  item: Zhang J

ReferenceForCatalyticMechanism
reference index: 11
reference section: p.3534

ReferenceForCatalyticMechanism
reference index: 13
reference section: Fig.1, p.9137
reference step: 2

ReferenceForCatalyticMechanism
reference index: 14
reference section: Fig.2, p.9148-9149

ReferenceForCatalyticMechanism
reference index: 17
reference section: Fig.5, p.312
reference step: 3

ReferenceForCatalyticMechanism
reference index: 18
reference section: p.1855