7R09

Amine Dehydrogenase MATOUAmDH2 in complex with NADP+ and Cyclohexylamine

7R09 の概要

• エントリーDOI: 10.2210/pdb7r09/pdb
• 分子名称: Amine Dehydrogenase, NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE, CYCLOHEXYLAMMONIUM ION, ... (4 entities in total)
• 機能のキーワード: amine, nadp, oxidoreductase
• 由来する生物種: metagenome
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 39092.92

構造登録者

Bennett, M.,Ducrot, L.,Vaxelaire-Vergne, C.,Grogan, G. (登録日: 2022-02-01, 公開日: 2022-04-06, 最終更新日: 2024-01-31)

主引用文献

Bennett, M.,Ducrot, L.,Vergne-Vaxelaire, C.,Grogan, G.
Structure and Mutation of the Native Amine Dehydrogenase MATOUAmDH2.
Chembiochem, 23:e202200136-e202200136, 2022

PubMed Abstract: Native amine dehydrogenases (nat-AmDHs) have recently emerged as a potentially valuable new reservoir of enzymes for the sustainable and selective synthesis of chiral amines, catalyzing the NAD(P)H-dependent ammoniation of carbonyl compounds with high activity and selectivity. MATOUAmDH2, recently identified from the Marine Atlas of Tara Oceans Unigenes (MATOUv1) database of eukaryotic genes, displays exceptional catalytic performance against its best identified substrate, isobutyraldehyde, as well as having broader substrate scope than other nat-AmDHs. In the interests of providing a platform for the rational engineering of this and other nat-AmDHs, we have determined the structure of MATOUAmDH2 in complex with NADP and also with the cofactor and cyclohexylamine. Monomers within the structure are representative of more open and closed conformations of the enzyme and illustrate the profound changes undergone by nat-AmDHs during the catalytic cycle. An alanine screen of active site residues revealed that M215A and L180A are more active than the wild-type enzyme for the amination of cyclohexanone with ammonia and methylamine respectively; the latter suggests that AmDHs have the potential to be engineered for the improved production of secondary amines.

PubMed: 35349204
DOI: 10.1002/cbic.202200136

実験手法

X-RAY DIFFRACTION (2.08 Å)