5FJN
Structure of L-Amino acid deaminase from Proteus myxofaciens in complex with anthranilate
Summary for 5FJN
| Entry DOI | 10.2210/pdb5fjn/pdb |
| Related | 5FJM |
| Descriptor | L-AMINO ACID DEAMINASE, FLAVIN-ADENINE DINUCLEOTIDE, 2-AMINOBENZOIC ACID, ... (4 entities in total) |
| Functional Keywords | hydrolase, l-amino acid deaminase, flavoprotein, flavoenzyme, membrane protein |
| Biological source | PROTEUS MYXOFACIENS |
| Total number of polymer chains | 2 |
| Total formula weight | 101936.65 |
| Authors | Motta, P.,Molla, G.,Pollegioni, L.,Nardini, M. (deposition date: 2015-10-11, release date: 2016-04-06, Last modification date: 2024-01-10) |
| Primary citation | Motta, P.,Molla, G.,Pollegioni, L.,Nardini, M. Structure-Function Relationships in L-Amino Acid Deaminase, a Flavoprotein Belonging to a Novel Class of Biotechnologically Relevant Enzymes J.Biol.Chem., 291:10457-, 2016 Cited by PubMed Abstract: l-Amino acid deaminase from Proteus myxofaciens (PmaLAAD) is a membrane flavoenzyme that catalyzes the deamination of neutral and aromatic l-amino acids into α-keto acids and ammonia. PmaLAAD does not use dioxygen to re-oxidize reduced FADH2 and thus does not produce hydrogen peroxide; instead, it uses a cytochrome b-like protein as an electron acceptor. Although the overall fold of this enzyme resembles that of known amine or amino acid oxidases, it shows the following specific structural features: an additional novel α+β subdomain placed close to the putative transmembrane α-helix and to the active-site entrance; an FAD isoalloxazine ring exposed to solvent; and a large and accessible active site suitable to bind large hydrophobic substrates. In addition, PmaLAAD requires substrate-induced conformational changes of part of the active site, particularly in Arg-316 and Phe-318, to achieve the correct geometry for catalysis. These studies are expected to pave the way for rationally improving the versatility of this flavoenzyme, which is critical for biocatalysis of enantiomerically pure amino acids. PubMed: 27022028DOI: 10.1074/JBC.M115.703819 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.75 Å) |
Structure validation
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