4QYJ

Structure of Phenylacetaldehyde Dehydrogenase from Pseudomonas putida S12

4QYJ の概要

• エントリーDOI: 10.2210/pdb4qyj/pdb
• 分子名称: Aldehyde dehydrogenase (1 entity in total)
• 機能のキーワード: aldehyde dehydrogenase, oxidoreductase
• 由来する生物種: Pseudomonas putida
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 440372.56

構造登録者

Crabo, A.G.,Gassner, G.T.,Sazinsky, M.H. (登録日: 2014-07-24, 公開日: 2015-08-19, 最終更新日: 2024-02-28)

主引用文献

Crabo, A.G.,Singh, B.,Nguyen, T.,Emami, S.,Gassner, G.T.,Sazinsky, M.H.
Structure and biochemistry of phenylacetaldehyde dehydrogenase from the Pseudomonas putida S12 styrene catabolic pathway.
Arch.Biochem.Biophys., 616:47-58, 2017

PubMed Abstract: Phenylacetaldehyde dehydrogenase catalyzes the NAD-dependent oxidation of phenylactealdehyde to phenylacetic acid in the styrene catabolic and detoxification pathway of Pseudomonas putida (S12). Here we report the structure and mechanistic properties of the N-terminally histidine-tagged enzyme, NPADH. The 2.83 Å X-ray crystal structure is similar in fold to sheep liver cytosolic aldehyde dehydrogenase (ALDH1), but has unique set of intersubunit interactions and active site tunnel for substrate entrance. In solution, NPADH occurs as 227 kDa homotetramer. It follows a sequential reaction mechanism in which NAD serves as both the leading substrate and homotropic allosteric activator. In the absence of styrene monooxygenase reductase, which regenerates NAD from NADH in the first step of styrene catabolism, NPADH is inhibited by a ternary complex involving NADH, product, and phenylacetaldehyde, substrate. Each oligomerization domain of NPADH contains a six-residue insertion that extends this loop over the substrate entrance tunnel of a neighboring subunit, thereby obstructing the active site of the adjacent subunit. This feature could be an important factor in the homotropic activation and product inhibition mechanisms. Compared to ALDH1, the substrate channel of NPADH is narrower and lined with more aromatic residues, suggesting a means for enhancing substrate specificity.

PubMed: 28153386
DOI: 10.1016/j.abb.2017.01.011

実験手法

X-RAY DIFFRACTION (2.83 Å)