Enzyme

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     4. Lyases
        4.3 Carbon-nitrogen lyases
            4.3.1 Ammonia-lyases
ID:4.3.1.17
Description:L-serine ammonia-lyase.
Alternative Name: Serine deaminase.
L-serine hydro-lyase (deaminating).
L-serine dehydratase.
L-serine deaminase.
L-hydroxyaminoacid dehydratase.
Prosite: PDOC00149;
PDB:
PDBScop
Cath: 3.30.1330.40; 3.30.1330.90; 3.40.1020.10; 3.40.50.1100;

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 4.3.1.17
BRENDA Enzyme Link: BRENDA 4.3.1.17
KEGG Enzyme Link: KEGG4.3.1.17
BioCyc Enzyme Link: BioCyc 4.3.1.17
ExPASy Enzyme Link: ExPASy4.3.1.17
EC2PDB Enzyme Link: EC2PDB 4.3.1.17
ExplorEnz Enzyme Link: ExplorEnz 4.3.1.17
PRIAM enzyme-specific profiles Link: PRIAM 4.3.1.17
IntEnz Enzyme Link: IntEnz 4.3.1.17
MEDLINE Enzyme Link: MEDLINE 4.3.1.17
MSA:

4.3.1.17;

Phylogenetic Tree:

4.3.1.17;

Uniprot:
M-CSA:
RHEA:19169 L-serine = NH4(+) + pyruvate
RULE(radius=1) [*:1]-[CH;+0:2](-[NH2;+0:3])-[CH2;+0:4]-[OH;+0:5]>>[*:1]-[C;H0;+0:2](-[CH3;+0:4])=[O;H0;+0:5].[NH3;+0:3]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Crystal structure of a homolog of mammalian serine racemase from Schizosaccharomyces pombe.Goto M, Yamauchi T, Kamiya N, Miyahara I, Yoshimura T, Mihara H, Kurihara T, Hirotsu K, Esaki N2009 Sep 1819640845
Crystal structure of serine dehydratase from rat liver.Yamada T, Komoto J, Takata Y, Ogawa H, Pitot HC, Takusagawa F2003 Nov 1114596599
A catalytic mechanism that explains a low catalytic activity of serine dehydratase like-1 from human cancer cells: crystal structure and site-directed mutagenesis studies.Yamada T, Komoto J, Kasuya T, Takata Y, Ogawa H, Mori H, Takusagawa F2008 May18342636