EzCatDB: T00095

DB codeT00095
CATH domainDomain 11.10.275.10Catalytic domain
Domain 21.20.200.10Catalytic domain
Domain 31.10.40.30
E.C.4.3.2.2
CSA1c3c
MACiEM0080

CATH domainRelated DB codes (homologues)
1.10.275.10D00267,T00086,T00092,T00094
1.10.40.30T00086,T00092,T00094
1.20.200.10D00267,T00086,T00092,T00094

Enzyme Name
Swiss-protKEGG

Q8ZY28Q9X0I0
Protein name
Adenylosuccinate lyaseadenylosuccinate lyase
adenylosuccinase
succino AMP-lyase
6-N-(1,2-dicarboxyethyl)AMP AMP-lyase
6-N-(1,2-dicarboxyethyl)AMP AMP-lyase (fumarate-forming)
SynonymsAdenylosuccinate lyase (PurB)
ASL
EC 4.3.2.2
Adenylosuccinase
ASase

KEGG pathways
MAP codePathways
MAP00230Purine metabolism
MAP00252Alanine and aspartate metabolism

Swiss-prot:Accession NumberQ8ZY28Q9X0I0
Entry nameQ8ZY28_PYRAEPUR8_THEMA
Activity
N(6)-(1,2-dicarboxyethyl)AMP = fumarate + AMP.,(S)-2-(5-amino-1-(5-phospho-D- ribosyl)imidazole-4-carboxamido)succinate = fumarate + 5-amino-1- (5-phospho-D-ribosyl)imidazole-4-carboxamide.
Subunit

Subcellular location

Cofactor



SubstratesProducts
KEGG-idC03794C04823C00122C00020C04677
CompoundN6-(1,2-Dicarboxyethyl)-AMP1-(5'-Phosphoribosyl)-4-(N-succinocarboxamide)-5-aminoimidazoleFumarateAMP1-(5'-Phosphoribosyl)-5-amino-4-imidazolecarboxamide
Typeamino acids,carboxyl group,nucleotideamino acids,amide group,amine group,carbohydrate,nucleotidecarboxyl groupamine group,nucleotideamide group,amine group,nucleotide
1dofA01UnboundUnboundUnboundUnboundUnbound
1dofB01UnboundUnboundUnboundUnboundUnbound
1dofC01UnboundUnboundUnboundUnboundUnbound
1dofD01UnboundUnboundUnboundUnboundUnbound
1c3cA01UnboundUnboundUnboundUnboundUnbound
1c3cB01UnboundUnboundUnboundUnboundUnbound
1c3uA01UnboundUnboundUnboundUnboundUnbound
1c3uB01UnboundUnboundUnboundUnboundUnbound
1dofA02UnboundUnboundUnboundUnboundUnbound
1dofB02UnboundUnboundUnboundUnboundUnbound
1dofC02UnboundUnboundUnboundUnboundUnbound
1dofD02UnboundUnboundUnboundUnboundUnbound
1c3cA02UnboundUnboundUnboundUnboundUnbound
1c3cB02UnboundUnboundUnboundUnboundUnbound
1c3uA02UnboundUnboundUnboundUnboundUnbound
1c3uB02UnboundUnboundUnboundUnboundUnbound
1dofA03UnboundUnboundUnboundUnboundUnbound
1dofB03UnboundUnboundUnboundUnboundUnbound
1dofC03UnboundUnboundUnboundUnboundUnbound
1dofD03UnboundUnboundUnboundUnboundUnbound
1c3cA03UnboundUnboundUnboundUnboundUnbound
1c3cB03UnboundUnboundUnboundUnboundUnbound
1c3uA03UnboundUnboundUnboundUnboundUnbound
1c3uB03UnboundUnboundUnboundUnboundUnbound

Active-site residues
resource
Swiss-prot;Q9X0I0 & literature [5] & [9]
pdbCatalytic residuescomment
1dofA01HIS 72
invisible 64-71
1dofB01HIS 72
invisible 64-71
1dofC01HIS 72
invisible 64-71
1dofD01HIS 72
invisible 64-71
1c3cA01HIS 68

1c3cB01HIS 68

1c3uA01HIS 68

1c3uB01HIS 68

1dofA02HIS 143;GLU 275
invisible 260-268
1dofB02HIS 143;GLU 275
invisible 260-268
1dofC02HIS 143;GLU 275
invisible 260-268
1dofD02HIS 143;GLU 275
invisible 260-268
1c3cA02HIS 141;GLU 275

1c3cB02HIS 141;GLU 275

1c3uA02HIS 141;GLU 275

1c3uB02HIS 141;GLU 275

1dofA03

1dofB03

1dofC03

1dofD03

1c3cA03

1c3cB03

1c3uA03

1c3uB03


References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[2]Fig.1, p.660-661
[8]Fig.5c, p.166-1692
[9]p.2224

references
[1]
PubMed ID3759987
JournalJ Biol Chem
Year1986
Volume261
Pages13637-42
AuthorsCasey PJ, Abeles RH, Lowenstein JM
TitleMetabolism of threo-beta-fluoroaspartate by H4 cells. Inhibition of adenylosuccinate lyase by fluoro analogs of its substrates.
[2]
CommentsHomologous enzymes
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.
[3]
PubMed ID8969519
JournalMicrobiology
Year1996
Volume142
Pages3219-30
AuthorsGreen SM, Malik T, Giles IG, Drabble WT
TitleThe purB gene of Escherichia coli K-12 is located in an operon.
[4]
PubMed ID8845770
JournalProtein Sci
Year1996
Volume5
Pages786-8
AuthorsRedinbo MR, Eide SM, Stone RL, Dixon JE, Yeates TO
TitleCrystallization and preliminary structural analysis of Bacillus subtilis adenylosuccinate lyase, an enzyme implicated in infantile autism.
[5]
PubMed ID9890879
JournalBiochemistry
Year1999
Volume38
Pages22-32
AuthorsLee TT, Worby C, Bao ZQ, Dixon JE, Colman RF
TitleHis68 and His141 are critical contributors to the intersubunit catalytic site of adenylosuccinate lyase of Bacillus subtilis.
[6]
PubMed ID11063569
JournalBiochemistry
Year2000
Volume39
Pages13336-43
AuthorsBrosius JL, Colman RF
TitleA key role in catalysis for His89 of adenylosuccinate lyase of Bacillus subtilis.
[7]
PubMed ID10926519
JournalJ Mol Biol
Year2000
Volume301
Pages433-50
AuthorsToth EA, Worby C, Dixon JE, Goedken ER, Marqusee S, Yeates TO
TitleThe crystal structure of adenylosuccinate lyase from Pyrobaculum aerophilum reveals an intracellular protein with three disulfide bonds.
Related PDB1dof
[8]
CommentsX-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
Medline ID20139703
PubMed ID10673438
JournalStructure Fold Des
Year2000
Volume8
Pages163-74
AuthorsToth EA, Yeates TO
TitleThe structure of adenylosuccinate lyase, an enzyme with dual activity in the de novo purine biosynthetic pathway.
Related PDB1c3c,1c3u
Related Swiss-protQ9X0I0
[9]
PubMed ID11841213
JournalBiochemistry
Year2002
Volume41
Pages2217-26
AuthorsBrosius JL, Colman RF
TitleThree subunits contribute amino acids to the active site of tetrameric adenylosuccinate lyase: Lys268 and Glu275 are required.

comments
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.

createdupdated
2004-06-282009-04-03


Copyright: Nozomi Nagano, JST & CBRC-AIST
Funded by PRESTO/Japan Science and Technology Corporation (JST) (December 2001 - November 2004)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2006)
Funded by Grant-in-Aid for Scientific Research (B)/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2008)
Funded by BIRD/Japan Science and Technology Corporation (JST) (September 2005 - September 2010)
Funded by BIRD/Japan Science and Technology Corporation (JST) (October 2007 - September 2010)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2011 - March 2012)

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