EzCatDB: T00092
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DB codeT00092
CATH domainDomain 11.10.275.10 : Fumarase C; Chain B, domain 1
Domain 21.20.200.10 : Fumarase C; Chain A, domain 2Catalytic domain
Domain 31.10.40.30 : Ribonucleotide Reductase Protein R1; domain 1
E.C.4.3.1.1

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

Enzyme Name
UniProtKBKEGG

P0AC38
Protein nameAspartate ammonia-lyaseaspartate ammonia-lyase
aspartase
fumaric aminase
L-aspartase
L-aspartate ammonia-lyase
SynonymsAspartase
EC 4.3.1.1
RefSeqNP_418562.4 (Protein)
NC_000913.2 (DNA/RNA sequence)
YP_492282.1 (Protein)
NC_007779.1 (DNA/RNA sequence)
PfamPF10415 (FumaraseC_C)
PF00206 (Lyase_1)
[Graphical view]

KEGG pathways
MAP codePathways
MAP00252Alanine and aspartate metabolism
MAP00910Nitrogen metabolism

UniProtKB:Accession NumberP0AC38
Entry nameASPA_ECOLI
ActivityL-aspartate = fumarate + NH(3).
SubunitHomotetramer.
Subcellular location
Cofactor

Compound table: links to PDB-related databases & PoSSuM

SubstratesProducts
KEGG-idC00049C00122C00014
CompoundL-AspartateFumarateNH3
Typeamino acids,carboxyl groupcarboxyl groupamine group,organic ion
ChEBI17053
18012
16134
PubChem5960
44367445
444972
21883788
222
           
1jswA01UnboundUnboundUnbound
1jswB01UnboundUnboundUnbound
1jswC01UnboundUnboundUnbound
1jswD01UnboundUnboundUnbound
1jswA02UnboundUnboundUnbound
1jswB02UnboundUnboundUnbound
1jswC02UnboundUnboundUnbound
1jswD02UnboundUnboundUnbound
1jswA03UnboundUnboundUnbound
1jswB03UnboundUnboundUnbound
1jswD03UnboundUnboundUnbound

Active-site residues
resource
literatyre [17]
pdbCatalytic residues
         
1jswA01 
1jswB01 
1jswC01 
1jswD01 
1jswA02SER 143
1jswB02SER 143
1jswC02SER 143
1jswD02SER 143
1jswA03 
1jswB03 
1jswD03 

References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[11]p.3534
[13]Fig.1, p.91372
[14]Fig.2, p.9148-9149
[17]Fig.5, p.3123
[18]p.1855

references
[1]
PubMed ID240429
JournalBiochim Biophys Acta
Year1975
Volume403
Pages221-31
AuthorsMizuta K, Tokushige M
TitleStudies on aspartase. II. Role of sulfhydryl groups in aspartase from Escherichia coli.
[2]
PubMed ID339956
JournalBiochim Biophys Acta
Year1978
Volume522
Pages243-50
AuthorsTokushige M, Eguchi G
TitleStudies on aspartase. V. Denaturant-mediated reactivation of aspartase, which has been otherwise irreversibly inactivated by various causes.
[3]
PubMed ID6357281
JournalBiochim Biophys Acta
Year1983
Volume749
Pages101-5
AuthorsYumoto N, Tokushige M
TitleAcetylation-induced alteration of catalytic and regulatory properties of aspartase.
[4]
PubMed ID2853974
JournalBiochemistry
Year1988
Volume27
Pages9089-93
AuthorsFalzone CJ, Karsten WE, Conley JD, Viola RE
TitleL-aspartase from Escherichia coli: substrate specificity and role of divalent metal ions.
[5]
PubMed ID3371801
JournalFolia Microbiol (Praha)
Year1988
Volume33
Pages101-7
AuthorsMalanik V, Malanikova M, Psenicka I, Sojkova I, Marek M
TitleEffect of detergents on aspartate ammonia-lyase activity in Escherichia alcalescens.
[6]
PubMed ID2043125
JournalBiochem Biophys Res Commun
Year1991
Volume177
Pages414-9
AuthorsMurase S, Takagi JS, Higashi Y, Imaishi H, Yumoto N, Tokushige M
TitleActivation of aspartase by site-directed mutagenesis.
[7]
PubMed ID8216244
JournalBiochem Biophys Res Commun
Year1993
Volume195
Pages1159-64
AuthorsMurase S, Kawata Y, Yumoto N
TitleUse of hybridization for distance measurement by fluorescence energy transfer in oligomeric proteins: distance between two functional sites in aspartase.
[8]
PubMed ID8478318
JournalJ Bacteriol
Year1993
Volume175
Pages2501-6
AuthorsSun D, Setlow P
TitleCloning and nucleotide sequence of the Bacillus subtilis ansR gene, which encodes a repressor of the ans operon coding for L-asparaginase and L-aspartase.
[9]
PubMed ID8113229
JournalJ Biochem (Tokyo)
Year1993
Volume114
Pages735-9
AuthorsMurase S, Yumoto N
TitleCharacterization of three types of aspartase activated by site-directed mutagenesis, limited proteolysis, and acetylation.
[10]
PubMed ID8263924
JournalJ Mol Biol
Year1993
Volume234
Pages1248-9
AuthorsShi W, Kidd R, Giorgianni F, Schindler JF, Viola RE, Farber GK
TitleCrystallization and preliminary X-ray studies of L-aspartase from Escherichia coli.
[11]
PubMed ID7893648
JournalBiochemistry
Year1995
Volume34
Pages3529-35
AuthorsGiorgianni F, Beranova S, Wesdemiotis C, Viola RE
TitleElimination of the sensitivity of L-aspartase to active-site-directed inactivation without alteration of catalytic activity.
[12]
PubMed ID7552727
JournalNat Struct Biol
Year1995
Volume2
Pages654-62
AuthorsWeaver TM, Levitt DG, Donnelly MI, Stevens PP, Banaszak LJ
TitleThe multisubunit active site of fumarase C from Escherichia coli.
[13]
CommentsX-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS)
Medline ID97375637
PubMed ID9230045
JournalBiochemistry
Year1997
Volume36
Pages9136-44
AuthorsShi W, Dunbar J, Jayasekera MM, Viola RE, Farber GK
TitleThe structure of L-aspartate ammonia-lyase from Escherichia coli.
Related PDB1jsw
Related UniProtKBP0AC38
[14]
PubMed ID9230046
JournalBiochemistry
Year1997
Volume36
Pages9145-50
AuthorsJayasekera MM, Shi W, Farber GK, Viola RE
TitleEvaluation of functionally important amino acids in L-aspartate ammonia-lyase from Escherichia coli.
[15]
PubMed ID9928150
JournalAnn N Y Acad Sci
Year1998
Volume864
Pages631-5
AuthorsLu J, Zhang J, Zhang H, Wang X
TitleStudies on the properties of mutants of aspartase from Escherichia coli W.
[16]
PubMed ID10529408
JournalBiochem Biophys Res Commun
Year1999
Volume264
Pages596-600
AuthorsJayasekera MM, Viola RE
TitleRecovery of catalytic activity from an inactive aggregated mutant of l-aspartase.
[17]
PubMed ID10800598
JournalAdv Enzymol Relat Areas Mol Biol
Year2000
Volume74
Pages295-341
AuthorsViola RE
TitleL-aspartase: new tricks from an old enzyme.
[18]
PubMed ID10712618
JournalEur J Biochem
Year2000
Volume267
Pages1847-57
AuthorsKawata Y, Tamura K, Kawamura M, Ikei K, Mizobata T, Nagai J, Fujita M, Yano S, Tokushige M, Yumoto N
TitleCloning and over-expression of thermostable Bacillus sp. YM55-1 aspartase and site-directed mutagenesis for probing a catalytic residue.
[19]
PubMed ID11983692
JournalJ Biol Chem
Year2002
Volume277
Pages24289-93
AuthorsKong X, Li Z, Gou X, Zhu S, Zhang H, Wang X, Zhang J
TitleA monomeric L-aspartase obtained by in vitro selection.

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]).

createdupdated
2004-06-232009-02-26


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