DB code: T00092

CATH domain 1.10.275.10 : Fumarase C; Chain B, domain 1
1.20.200.10 : Fumarase C; Chain A, domain 2 Catalytic domain
1.10.40.30 : Ribonucleotide Reductase Protein R1; domain 1
E.C. 4.3.1.1
CSA
M-CSA
MACiE

CATH domain Related DB codes (homologues)
1.10.275.10 : Fumarase C; Chain B, domain 1 D00267 T00086 T00094 T00095
1.10.40.30 : Ribonucleotide Reductase Protein R1; domain 1 T00086 T00094 T00095
1.20.200.10 : Fumarase C; Chain A, domain 2 D00267 T00086 T00094 T00095

Uniprot Enzyme Name
UniprotKB Protein name Synonyms RefSeq Pfam
P0AC38 Aspartate ammonia-lyase
Aspartase
EC 4.3.1.1
NP_418562.4 (Protein)
NC_000913.2 (DNA/RNA sequence)
YP_492282.1 (Protein)
NC_007779.1 (DNA/RNA sequence)
PF10415 (FumaraseC_C)
PF00206 (Lyase_1)
[Graphical View]

KEGG enzyme name
aspartate ammonia-lyase
aspartase
fumaric aminase
L-aspartase
L-aspartate ammonia-lyase

UniprotKB: Accession Number Entry name Activity Subunit Subcellular location Cofactor
P0AC38 ASPA_ECOLI L-aspartate = fumarate + NH(3). Homotetramer.

KEGG Pathways
Map code Pathways E.C.
MAP00252 Alanine and aspartate metabolism
MAP00910 Nitrogen metabolism

Compound table
Substrates Products Intermediates
KEGG-id C00049 C00122 C00014
E.C.
Compound L-Aspartate Fumarate NH3
Type amino acids,carboxyl group carboxyl group amine group,organic ion
ChEBI 17053
18012
16134
PubChem 44367445
5960
21883788
444972
222
1jswA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound
1jswB01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound
1jswC01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound
1jswD01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound
1jswA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound
1jswB02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound
1jswC02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound
1jswD02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound
1jswA03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound
1jswB03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound
1jswD03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound

Reference for Active-site residues
resource references E.C.
literatyre [17]

Active-site residues
PDB Catalytic residues Cofactor-binding residues Modified residues Main-chain involved in catalysis Comment
1jswA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1jswB01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1jswC01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1jswD01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1jswA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain SER 143
1jswB02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain SER 143
1jswC02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain SER 143
1jswD02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain SER 143
1jswA03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1jswB03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1jswD03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain

References for Catalytic Mechanism
References Sections No. of steps in catalysis
[11]
p.3534
[13]
Fig.1, p.9137 2
[14]
Fig.2, p.9148-9149
[17]
Fig.5, p.312 3
[18]
p.1855

References
[1]
Resource
Comments
Medline ID
PubMed ID 240429
Journal Biochim Biophys Acta
Year 1975
Volume 403
Pages 221-31
Authors Mizuta K, Tokushige M
Title Studies on aspartase. II. Role of sulfhydryl groups in aspartase from Escherichia coli.
Related PDB
Related UniProtKB
[2]
Resource
Comments
Medline ID
PubMed ID 339956
Journal Biochim Biophys Acta
Year 1978
Volume 522
Pages 243-50
Authors Tokushige M, Eguchi G
Title Studies on aspartase. V. Denaturant-mediated reactivation of aspartase, which has been otherwise irreversibly inactivated by various causes.
Related PDB
Related UniProtKB
[3]
Resource
Comments
Medline ID
PubMed ID 6357281
Journal Biochim Biophys Acta
Year 1983
Volume 749
Pages 101-5
Authors Yumoto N, Tokushige M
Title Acetylation-induced alteration of catalytic and regulatory properties of aspartase.
Related PDB
Related UniProtKB
[4]
Resource
Comments
Medline ID
PubMed ID 2853974
Journal Biochemistry
Year 1988
Volume 27
Pages 9089-93
Authors Falzone CJ, Karsten WE, Conley JD, Viola RE
Title L-aspartase from Escherichia coli: substrate specificity and role of divalent metal ions.
Related PDB
Related UniProtKB
[5]
Resource
Comments
Medline ID
PubMed ID 3371801
Journal Folia Microbiol (Praha)
Year 1988
Volume 33
Pages 101-7
Authors Malanik V, Malanikova M, Psenicka I, Sojkova I, Marek M
Title Effect of detergents on aspartate ammonia-lyase activity in Escherichia alcalescens.
Related PDB
Related UniProtKB
[6]
Resource
Comments
Medline ID
PubMed ID 2043125
Journal Biochem Biophys Res Commun
Year 1991
Volume 177
Pages 414-9
Authors Murase S, Takagi JS, Higashi Y, Imaishi H, Yumoto N, Tokushige M
Title Activation of aspartase by site-directed mutagenesis.
Related PDB
Related UniProtKB
[7]
Resource
Comments
Medline ID
PubMed ID 8216244
Journal Biochem Biophys Res Commun
Year 1993
Volume 195
Pages 1159-64
Authors Murase S, Kawata Y, Yumoto N
Title Use of hybridization for distance measurement by fluorescence energy transfer in oligomeric proteins: distance between two functional sites in aspartase.
Related PDB
Related UniProtKB
[8]
Resource
Comments
Medline ID
PubMed ID 8478318
Journal J Bacteriol
Year 1993
Volume 175
Pages 2501-6
Authors Sun D, Setlow P
Title 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.
Related PDB
Related UniProtKB
[9]
Resource
Comments
Medline ID
PubMed ID 8113229
Journal J Biochem (Tokyo)
Year 1993
Volume 114
Pages 735-9
Authors Murase S, Yumoto N
Title Characterization of three types of aspartase activated by site-directed mutagenesis, limited proteolysis, and acetylation.
Related PDB
Related UniProtKB
[10]
Resource
Comments
Medline ID
PubMed ID 8263924
Journal J Mol Biol
Year 1993
Volume 234
Pages 1248-9
Authors Shi W, Kidd R, Giorgianni F, Schindler JF, Viola RE, Farber GK
Title Crystallization and preliminary X-ray studies of L-aspartase from Escherichia coli.
Related PDB
Related UniProtKB
[11]
Resource
Comments
Medline ID
PubMed ID 7893648
Journal Biochemistry
Year 1995
Volume 34
Pages 3529-35
Authors Giorgianni F, Beranova S, Wesdemiotis C, Viola RE
Title Elimination of the sensitivity of L-aspartase to active-site-directed inactivation without alteration of catalytic activity.
Related PDB
Related UniProtKB
[12]
Resource
Comments
Medline ID
PubMed ID 7552727
Journal Nat Struct Biol
Year 1995
Volume 2
Pages 654-62
Authors Weaver TM, Levitt DG, Donnelly MI, Stevens PP, Banaszak LJ
Title The multisubunit active site of fumarase C from Escherichia coli.
Related PDB
Related UniProtKB
[13]
Resource
Comments X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS)
Medline ID 97375637
PubMed ID 9230045
Journal Biochemistry
Year 1997
Volume 36
Pages 9136-44
Authors Shi W, Dunbar J, Jayasekera MM, Viola RE, Farber GK
Title The structure of L-aspartate ammonia-lyase from Escherichia coli.
Related PDB 1jsw
Related UniProtKB P0AC38
[14]
Resource
Comments
Medline ID
PubMed ID 9230046
Journal Biochemistry
Year 1997
Volume 36
Pages 9145-50
Authors Jayasekera MM, Shi W, Farber GK, Viola RE
Title Evaluation of functionally important amino acids in L-aspartate ammonia-lyase from Escherichia coli.
Related PDB
Related UniProtKB
[15]
Resource
Comments
Medline ID
PubMed ID 9928150
Journal Ann N Y Acad Sci
Year 1998
Volume 864
Pages 631-5
Authors Lu J, Zhang J, Zhang H, Wang X
Title Studies on the properties of mutants of aspartase from Escherichia coli W.
Related PDB
Related UniProtKB
[16]
Resource
Comments
Medline ID
PubMed ID 10529408
Journal Biochem Biophys Res Commun
Year 1999
Volume 264
Pages 596-600
Authors Jayasekera MM, Viola RE
Title Recovery of catalytic activity from an inactive aggregated mutant of l-aspartase.
Related PDB
Related UniProtKB
[17]
Resource
Comments
Medline ID
PubMed ID 10800598
Journal Adv Enzymol Relat Areas Mol Biol
Year 2000
Volume 74
Pages 295-341
Authors Viola RE
Title L-aspartase: new tricks from an old enzyme.
Related PDB
Related UniProtKB
[18]
Resource
Comments
Medline ID
PubMed ID 10712618
Journal Eur J Biochem
Year 2000
Volume 267
Pages 1847-57
Authors Kawata Y, Tamura K, Kawamura M, Ikei K, Mizobata T, Nagai J, Fujita M, Yano S, Tokushige M, Yumoto N
Title Cloning and over-expression of thermostable Bacillus sp. YM55-1 aspartase and site-directed mutagenesis for probing a catalytic residue.
Related PDB
Related UniProtKB
[19]
Resource
Comments
Medline ID
PubMed ID 11983692
Journal J Biol Chem
Year 2002
Volume 277
Pages 24289-93
Authors Kong X, Li Z, Gou X, Zhu S, Zhang H, Wang X, Zhang J
Title A monomeric L-aspartase obtained by in vitro selection.
Related PDB
Related UniProtKB

Comments
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]).

Created Updated
2004-06-23 2009-02-26