Brand  (β version)

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Ligands
Code Name Link
0JO 2-{[(E)-{3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylidene]amino}prop-2-enoic acid
Code : 4D9M   PDBj   RCSB PDB   PDBe
Header : LYASE
Title : Crystal structure of Diaminopropionate ammonia lyase from Escherichia coli in complex with aminoacrylate-PLP azomethine reaction intermediate
Release Data : 2012-04-25
Compound :
mol_id molecule chains synonym
1 Diaminopropionate ammonia-lyase A,B Diaminopropionatase, Alpha,beta-diaminopropionate ammonia-lyase
ec: 4.3.1.15
Source :
mol_id organism_scientific expression_system
1 Escherichia coli  (taxid:83333) Escherichia coli  (taxid:562)
strain: K12
gene: b2871, JW2839, ygeX
expression_system_strain: BL21(DE3)pLysS
expression_system_vector_type: PLASMID
expression_system_plasmid: pRSET-C
Authors : Bisht, S., Rajaram, V., Bharath, S.R., Murthy, M.R.N.
Keywords : Fold type II PLP-dependent enzyme, Tryptophan synthase beta subunit-like PLP-dependent enzymes superfamily, Lyase
Exp. method : X-RAY DIFFRACTION ( 2.50 Å )
Citation :

Crystal Structure of Escherichia coli Diaminopropionate Ammonia-lyase Reveals Mechanism of Enzyme Activation and Catalysis

Bisht, S.,Rajaram, V.,Bharath, S.R.  et al.
(2012)  J.Biol.Chem.  287 : 20369 - 20381

PubMed: 22505717
DOI: 10.1074/jbc.M112.351809

Chain : A, B
UniProt : P66899 (DPAL_ECOLI)
Reaction : Reaction=(S)-2,3-diaminopropanoate + H(+) + H2O = 2 NH4(+) + pyruvate; Xref=Rhea:RHEA:22084, ChEBI:CHEBI:15361, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28938, ChEBI:CHEBI:57721; EC=4.3.1.15; Evidence={ECO:0000269|PubMed:12596860};
Reaction=(R)-2,3-diaminopropanoate + H(+) + H2O = 2 NH4(+) + pyruvate; Xref=Rhea:RHEA:52432, ChEBI:CHEBI:15361, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28938, ChEBI:CHEBI:136599; EC=4.3.1.15; Evidence={ECO:0000269|PubMed:12596860};