1K1D

Crystal structure of D-hydantoinase

1K1D の概要

• エントリーDOI: 10.2210/pdb1k1d/pdb
• 分子名称: D-hydantoinase, ZINC ION (2 entities in total)
• 機能のキーワード: d-hydantoinase, hydrolase
• 由来する生物種: Geobacillus stearothermophilus
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 406115.51

構造登録者

Cheon, Y.H.,Kim, H.S.,Han, K.H.,Abendroth, J.,Niefind, K.,Schomburg, D.,Wang, J.,Kim, Y. (登録日: 2001-09-25, 公開日: 2002-08-14, 最終更新日: 2025-03-26)

主引用文献

Cheon, Y.H.,Kim, H.S.,Han, K.H.,Abendroth, J.,Niefind, K.,Schomburg, D.,Wang, J.,Kim, Y.
Crystal structure of D-hydantoinase from Bacillus stearothermophilus: insight into the stereochemistry of enantioselectivity.
Biochemistry, 41:9410-9417, 2002

PubMed Abstract: Industrial production of antibiotics, such as semisynthetic penicillins and cephalosporins, requires optically pure D-p-hydroxylphenylglycine and its derivatives as important side-chain precursors. To produce optically pure D-amino acids, microbial D-hydantoinase (E.C. 3.5.2.2) is used for stereospecific hydrolysis of chemically synthesized cyclic hydantoins. We report the apo-crystal structure of D-hydantoinase from B. stearothermophilus SD1 at 3.0 A resolution. The structure has a classic TIM barrel fold. Despite an undetectable similarity in sequence, D-hydantoinase shares a striking structural similarity with the recently solved structure of dihydroorotase. A structural comparison of hydantoinase with dihydroorotase revealed that the catalytic chemistry is conserved, while the substrate recognition is not. This structure provides insight into the stereochemistry of enantioselectivity in hydrolysis and illustrates how the enzyme recognizes stereospecific exocyclic substituents and hydrolyzes hydantoins. It should also provide a rationale for further directed evolution of this enzyme for hydrolysis of new hydantoins with novel exocyclic substituents.

PubMed: 12135362
DOI: 10.1021/bi0201567

実験手法

X-RAY DIFFRACTION (3.01 Å)