Enzyme

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     4. Lyases
        4.3 Carbon-nitrogen lyases
            4.3.1 Ammonia-lyases
ID:4.3.1.19
Description:Threonine ammonia-lyase.
Alternative Name: Threonine dehydratase.
Threonine dehydrase.
Threonine deaminase.
Serine deaminase.
L-threonine hydro-lyase (deaminating).
L-threonine dehydratase.
L-threonine deaminase.
L-serine 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 4.3.1.19
BRENDA Enzyme Link: BRENDA 4.3.1.19
KEGG Enzyme Link: KEGG4.3.1.19
BioCyc Enzyme Link: BioCyc 4.3.1.19
ExPASy Enzyme Link: ExPASy4.3.1.19
EC2PDB Enzyme Link: EC2PDB 4.3.1.19
ExplorEnz Enzyme Link: ExplorEnz 4.3.1.19
PRIAM enzyme-specific profiles Link: PRIAM 4.3.1.19
IntEnz Enzyme Link: IntEnz 4.3.1.19
MEDLINE Enzyme Link: MEDLINE 4.3.1.19
MSA:

4.3.1.19;

Phylogenetic Tree:

4.3.1.19;

Uniprot:
M-CSA:
RHEA:22108 L-threonine = 2-oxobutanoate + NH4(+)
RULE(radius=1) [*:1]-[CH;+0:2](-[NH2;+0:3])-[CH;+0:4](-[*:5])-[OH;+0:6]>>[*:1]-[C;H0;+0:2](=[O;H0;+0:6])-[CH2;+0:4]-[*:5].[NH3;+0:3]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Regulation of isoleucine-valine biosynthesis in Saccharomyces cerevisiae.Holmberg S, Petersen JG1988 Mar3289762
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
Elucidation of an alternate isoleucine biosynthesis pathway in Geobacter sulfurreducens.Risso C, Van Dien SJ, Orloff A, Lovley DR, Coppi MV2008 Apr18245290
Crystal structures of Salmonella typhimurium biodegradative threonine deaminase and its complex with CMP provide structural insights into ligand-induced oligomerization and enzyme activation.Simanshu DK, Savithri HS, Murthy MR2006 Dec 2217046821
Serine and threonine desaminaes of Escherichia coli; activators for a cell-free enzyme.WOOD WA, GUNSALUS IC1949 Nov15390404