1BW9

PHENYLALANINE DEHYDROGENASE STRUCTURE IN TERNARY COMPLEX WITH NAD+ AND PHENYLPYRUVATE

1BW9 の概要

• エントリーDOI: 10.2210/pdb1bw9/pdb
• 分子名称: PHENYLALANINE DEHYDROGENASE, NICOTINAMIDE-ADENINE-DINUCLEOTIDE, 3-PHENYLPYRUVIC ACID, ... (10 entities in total)
• 機能のキーワード: amino acid dehydrogenase, oxidative deamination mechanism
• 由来する生物種: Rhodococcus sp.; 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 75476.67

構造登録者

Vanhooke, J.L.,Thoden, J.B.,Brunhuber, N.M.W.,Blanchard, J.L.,Holden, H.M. (登録日: 1998-10-01, 公開日: 1999-05-18, 最終更新日: 2024-02-07)

主引用文献

Vanhooke, J.L.,Thoden, J.B.,Brunhuber, N.M.,Blanchard, J.S.,Holden, H.M.
Phenylalanine dehydrogenase from Rhodococcus sp. M4: high-resolution X-ray analyses of inhibitory ternary complexes reveal key features in the oxidative deamination mechanism.
Biochemistry, 38:2326-2339, 1999

PubMed Abstract: The molecular structures of recombinant L-phenylalanine dehydrogenase from Rhodococcus sp. M4 in two different inhibitory ternary complexes have been determined by X-ray crystallographic analyses to high resolution. Both structures show that L-phenylalanine dehydrogenase is a homodimeric enzyme with each monomer composed of distinct globular N- and C-terminal domains separated by a deep cleft containing the active site. The N-terminal domain binds the amino acid substrate and contributes to the interactions at the subunit:subunit interface. The C-terminal domain contains a typical Rossmann fold and orients the dinucleotide. The dimer has overall dimensions of approximately 82 A x 75 A x 75 A, with roughly 50 A separating the two active sites. The structures described here, namely the enzyme.NAD+.phenylpyruvate, and enzyme. NAD+.beta-phenylpropionate species, represent the first models for any amino acid dehydrogenase in a ternary complex. By analysis of the active-site interactions in these models, along with the currently available kinetic data, a detailed chemical mechanism has been proposed. This mechanism differs from those proposed to date in that it accounts for the inability of the amino acid dehydrogenases, in general, to function as hydroxy acid dehydrogenases.

PubMed: 10029526
DOI: 10.1021/bi982244q

実験手法

X-RAY DIFFRACTION (1.5 Å)