6CI8

Structure of the microcompartment-associated aminoacetone dehydrogenase

6CI8 の概要

• エントリーDOI: 10.2210/pdb6ci8/pdb
• 分子名称: 3-oxoacyl-[acyl-carrier-protein] reductase, CHLORIDE ION (3 entities in total)
• 機能のキーワード: dehydrogenase, short-chain dehydrogenase/reductase, oxidoreductase
• 由来する生物種: Mycobacterium smegmatis (strain ATCC 700084 / mc(2)155)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 54251.65

構造登録者

Mallette, E.,Kimber, M.S. (登録日: 2018-02-23, 公開日: 2018-05-30, 最終更新日: 2023-10-04)

主引用文献

Mallette, E.,Kimber, M.S.
Structure and Kinetics of the S-(+)-1-Amino-2-propanol Dehydrogenase from the RMM Microcompartment of Mycobacterium smegmatis.
Biochemistry, 57:3780-3789, 2018

PubMed Abstract: S-(+)-1-Amino-2-propanol dehydrogenase (APDH) is a short-chain dehydrogenase/reductase associated with the incompletely characterized Rhodococcus and Mycobacterium bacterial microcompartment (RMM). We enzymatically characterized the APDH from M. smegmatis and showed it is highly selective, with a low micromolar K for S-(+)-1-amino-2-propanol and specificity for NADP(H). A paralogous enzyme from a nonmicrocompartment-associated operon in the same organism was also shown to have a similar activity. We determined the structure of APDH in both apo form (at 1.7 Å) and as a ternary enzyme complex with NADP and aminoacetone (at 1.9 Å). Recognition of aminoacetone was mediated by strong hydrogen bonds to the amino group by Thr145 and by Glu251 from the C-terminus of an adjacent protomer. The substrate binding site entirely encloses the substrate, with close contacts between the aminoacetone methyl group and Phe95, Trp154, and Leu195. Kinetic characterization of several of these residues confirm their importance in enzyme functioning. Bioinformatics analysis of APDH homologues implies that many nonmicrocompartment APDH orthologues partake in an aminoacetone degradation pathway that proceeds via an aminopropanol O-phosphate phospholyase. RMM microcompartments may mediate a similar pathway, though possibly with differences in the details of the pathway that necessitates encapsulation behind a shell.

PubMed: 29757625
DOI: 10.1021/acs.biochem.8b00464

実験手法

X-RAY DIFFRACTION (1.7 Å)