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
 17053
 		18012
 18012
 		16134
 16134
PubChem 44367445
 5960
 44367445
 5960
 		21883788
 444972
 21883788
 444972
 		222
 222
1jswA01 Unbound Unbound Unbound
1jswB01 Unbound Unbound Unbound
1jswC01 Unbound Unbound Unbound
1jswD01 Unbound Unbound Unbound
1jswA02 Unbound Unbound Unbound
1jswB02 Unbound Unbound Unbound
1jswC02 Unbound Unbound Unbound
1jswD02 Unbound Unbound Unbound
1jswA03 Unbound Unbound Unbound
1jswB03 Unbound Unbound Unbound
1jswD03 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
1jswB01
1jswC01
1jswD01
1jswA02 SER 143
1jswB02 SER 143
1jswC02 SER 143
1jswD02 SER 143
1jswA03
1jswB03
1jswD03

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