Enzyme

Download
EC Tree
     4. Lyases
        4.3 Carbon-nitrogen lyases
            4.3.1 Ammonia-lyases
ID:4.3.1.15
Description:Diaminopropionate ammonia-lyase.
Alternative Name: Diaminopropionatase.
Alpha,beta-diaminopropionate ammonia-lyase.
2,3-diaminopropanoate ammonia-lyase.
Cath: 3.40.50.1100;

3D structure

Click one PDB to see exact 3D structure provided by NGL.

Note: Use your mouse to drag, rotate, and zoom in and out of the structure. Mouse-over to identify atoms and bonds. Mouse controls documentation.

References

External Links

UniProtKB Enzyme Link: UniProtKB 4.3.1.15
BRENDA Enzyme Link: BRENDA 4.3.1.15
KEGG Enzyme Link: KEGG4.3.1.15
BioCyc Enzyme Link: BioCyc 4.3.1.15
ExPASy Enzyme Link: ExPASy4.3.1.15
EC2PDB Enzyme Link: EC2PDB 4.3.1.15
ExplorEnz Enzyme Link: ExplorEnz 4.3.1.15
PRIAM enzyme-specific profiles Link: PRIAM 4.3.1.15
IntEnz Enzyme Link: IntEnz 4.3.1.15
MEDLINE Enzyme Link: MEDLINE 4.3.1.15
MSA:

4.3.1.15;

Phylogenetic Tree:

4.3.1.15;

Uniprot:
M-CSA:
RHEA:52432 (R)-2,3-diaminopropanoate + H(+) + H2O = 2 NH4(+) + pyruvate
RULE(radius=1) [*:1]-[CH;+0:2](-[NH2;+0:3])-[CH2;+0:4]-[NH2;+0:5].[H+;H0:6].[OH2;+0:7]>>[*:1]-[C;H0;+0:2](-[CH3;+0:4])=[O;H0;+0:7].[NH3;+0:3].[NH3;+0:5]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Diaminopropionate ammonia-lyase from Salmonella typhimurium. Purification and characterization of the crystalline enzyme, and sequence determination of the pyridoxal 5'-phosphate binding peptide.Nagasawa T, Tanizawa K, Satoda T, Yamada H1988 Jan 153275662
Crystal structure of Escherichia coli diaminopropionate ammonia-lyase reveals mechanism of enzyme activation and catalysis.Bisht S, Rajaram V, Bharath SR, Kalyani JN, Khan F, Rao AN, Savithri HS, Murthy MR2012 Jun 822505717

RHEA:22084 (S)-2,3-diaminopropanoate + H(+) + H2O = 2 NH4(+) + pyruvate
RULE(radius=1) [*:1]-[CH;+0:2](-[NH2;+0:3])-[CH2;+0:4]-[NH2;+0:5].[H+;H0:6].[OH2;+0:7]>>[*:1]-[C;H0;+0:2](-[CH3;+0:4])=[O;H0;+0:7].[NH3;+0:3].[NH3;+0:5]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Diaminopropionate ammonia-lyase from Salmonella typhimurium. Purification and characterization of the crystalline enzyme, and sequence determination of the pyridoxal 5'-phosphate binding peptide.Nagasawa T, Tanizawa K, Satoda T, Yamada H1988 Jan 153275662
Crystal structure of Escherichia coli diaminopropionate ammonia-lyase reveals mechanism of enzyme activation and catalysis.Bisht S, Rajaram V, Bharath SR, Kalyani JN, Khan F, Rao AN, Savithri HS, Murthy MR2012 Jun 822505717