5FJM

Structure of L-Amino acid deaminase from Proteus myxofaciens

5FJM の概要

• エントリーDOI: 10.2210/pdb5fjm/pdb
• 関連するPDBエントリー: 5FJN
• 分子名称: L-AMINO ACID DEAMINASE, FLAVIN-ADENINE DINUCLEOTIDE (3 entities in total)
• 機能のキーワード: hydrolase, l-amino acid deaminase, flavoprotein, flavoenzyme, membrane protein
• 由来する生物種: PROTEUS MYXOFACIENS
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 101662.38

構造登録者

Motta, P.,Molla, G.,Pollegioni, L.,Nardini, M. (登録日: 2015-10-11, 公開日: 2016-04-06, 最終更新日: 2024-01-10)

主引用文献

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

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: 27022028
DOI: 10.1074/JBC.M115.703819

実験手法

X-RAY DIFFRACTION (2 Å)