Enzyme

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     4. Lyases
        4.3 Carbon-nitrogen lyases
            4.3.1 Ammonia-lyases
ID:4.3.1.3
Description:Histidine ammonia-lyase.
Alternative Name: Histidine alpha-deaminase.
Histidinase.
Histidase.
Prosite: PDOC00424;
PDB:
PDBScop
1Y2M 8030021; 8042400; 8030021; 8042400; 8030021; 8042400; 8030021; 8042400;
1GK2 8023501; 8035881; 8023501; 8035881; 8023501; 8035881; 8023501; 8035881;
4C6G
4C5U
Cath: 1.10.274.20; 1.10.275.10; 1.20.200.10;

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 4.3.1.3
BRENDA Enzyme Link: BRENDA 4.3.1.3
KEGG Enzyme Link: KEGG4.3.1.3
BioCyc Enzyme Link: BioCyc 4.3.1.3
ExPASy Enzyme Link: ExPASy4.3.1.3
EC2PDB Enzyme Link: EC2PDB 4.3.1.3
ExplorEnz Enzyme Link: ExplorEnz 4.3.1.3
PRIAM enzyme-specific profiles Link: PRIAM 4.3.1.3
IntEnz Enzyme Link: IntEnz 4.3.1.3
MEDLINE Enzyme Link: MEDLINE 4.3.1.3
MSA:

4.3.1.3;

Phylogenetic Tree:

4.3.1.3;

Uniprot:
M-CSA:
RHEA:21232 L-histidine = NH4(+) + trans-urocanate
RULE(radius=1) [*:1]-[CH;+0:2](-[NH2;+0:3])-[CH2;+0:4]-[*:5]>>[*:1]-[CH;+0:2]=[CH;+0:4]-[*:5].[NH3;+0:3]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Friedel-Crafts-type mechanism for the enzymatic elimination of ammonia from histidine and phenylalanine.Poppe L, Rétey J2005 Jun 1315906398
Characterization of the active site of histidine ammonia-lyase from Pseudomonas putida.Röther D, Poppe L, Viergutz S, Langer B, Rétey J2001 Dec11732994