Enzyme

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     4. Lyases
        4.3 Carbon-nitrogen lyases
            4.3.2 Amidine-lyases
ID:4.3.2.2
Description:Adenylosuccinate lyase.
Alternative Name: Succino AMP-lyase.
Adenylosuccinase.
Prosite: PDOC00147;
PDB:
PDBScop
Cath: 1.10.275.10; 1.10.275.60; 1.10.40.30; 1.20.200.10; 1.20.5.3210;

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 4.3.2.2
BRENDA Enzyme Link: BRENDA 4.3.2.2
KEGG Enzyme Link: KEGG4.3.2.2
BioCyc Enzyme Link: BioCyc 4.3.2.2
ExPASy Enzyme Link: ExPASy4.3.2.2
EC2PDB Enzyme Link: EC2PDB 4.3.2.2
ExplorEnz Enzyme Link: ExplorEnz 4.3.2.2
PRIAM enzyme-specific profiles Link: PRIAM 4.3.2.2
IntEnz Enzyme Link: IntEnz 4.3.2.2
MEDLINE Enzyme Link: MEDLINE 4.3.2.2
MSA:

4.3.2.2;

Phylogenetic Tree:

4.3.2.2;

Uniprot:
M-CSA:
RHEA:23920 (2S)-2-[5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamido]succinate = 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + fumarate
RULE(radius=1) [*:1]-[CH;+0:2](-[CH2;+0:3]-[*:4])-[NH;+0:5]-[*:6]>>[*:1]-[CH;+0:2]=[CH;+0:3]-[*:4].[*:6]-[NH2;+0:5]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Structural and biochemical characterization of human adenylosuccinate lyase (ADSL) and the R303C ADSL deficiency-associated mutation.Ray SP, Deaton MK, Capodagli GC, Calkins LA, Sawle L, Ghosh K, Patterson D, Pegan SD2012 Aug 2122812634
Substrate and product complexes of Escherichia coli adenylosuccinate lyase provide new insights into the enzymatic mechanism.Tsai M, Koo J, Yip P, Colman RF, Segall ML, Howell PL2007 Jul 1317531264
Expression, purification, and characterization of stable, recombinant human adenylosuccinate lyase.Lee P, Colman RF2007 Feb16973378
Gln212, Asn270, and Arg301 are critical for catalysis by adenylosuccinate lyase from Bacillus subtilis.Segall ML, Colman RF2004 Jun 1515182182
Adenylosuccinate lyase from Artemia embryos. Purification and properties.Pinto RM, Faraldo A, Fernández A, Canales J, Sillero A, Sillero MA1983 Oct 256630197
Elucidation of the substrate specificity, kinetic and catalytic mechanism of adenylosuccinate lyase from Plasmodium falciparum.Bulusu V, Srinivasan B, Bopanna MP, Balaram H2009 Apr19111634
Effect of a new non-cleavable substrate analog on wild-type and serine mutants in the signature sequence of adenylosuccinate lyase of Bacillus subtilis and Homo sapiens.Sivendran S, Colman RF2008 Jul18469177
Escherichia coli purB gene: cloning, nucleotide sequence, and regulation by purR.He B, Smith JM, Zalkin H1992 Jan1729205

RHEA:16853 N(6)-(1,2-dicarboxyethyl)-AMP = AMP + fumarate
RULE(radius=1) [*:1]-[CH;+0:2](-[CH2;+0:3]-[*:4])-[NH;+0:5]-[*:6]>>[*:1]-[CH;+0:2]=[CH;+0:3]-[*:4].[*:6]-[NH2;+0:5]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Structural and biochemical characterization of human adenylosuccinate lyase (ADSL) and the R303C ADSL deficiency-associated mutation.Ray SP, Deaton MK, Capodagli GC, Calkins LA, Sawle L, Ghosh K, Patterson D, Pegan SD2012 Aug 2122812634
Substrate and product complexes of Escherichia coli adenylosuccinate lyase provide new insights into the enzymatic mechanism.Tsai M, Koo J, Yip P, Colman RF, Segall ML, Howell PL2007 Jul 1317531264
Expression, purification, and characterization of stable, recombinant human adenylosuccinate lyase.Lee P, Colman RF2007 Feb16973378
Gln212, Asn270, and Arg301 are critical for catalysis by adenylosuccinate lyase from Bacillus subtilis.Segall ML, Colman RF2004 Jun 1515182182