1ERZ

CRYSTAL STRUCTURE OF N-CARBAMYL-D-AMINO ACID AMIDOHYDROLASE WITH A NOVEL CATALYTIC FRAMEWORK COMMON TO AMIDOHYDROLASES

Summary for 1ERZ

• Entry DOI: 10.2210/pdb1erz/pdb
• Descriptor: N-CARBAMYL-D-AMINO ACID AMIDOHYDROLASE (2 entities in total)
• Functional Keywords: four-layer sandwich, hydrolase
• Biological source: Agrobacterium sp.
• Total number of polymer chains: 2
• Total formula weight: 68398.19

Authors

Nakai, T.,Hasegawa, T.,Yamashita, E.,Yamamoto, M.,Kumasaka, T.,Ueki, T.,Nanba, H.,Ikenaka, Y.,Takahashi, S.,Sato, M.,Tsukihara, T. (deposition date: 2000-04-06, release date: 2001-04-06, Last modification date: 2024-02-07)

Primary citation

Nakai, T.,Hasegawa, T.,Yamashita, E.,Yamamoto, M.,Kumasaka, T.,Ueki, T.,Nanba, H.,Ikenaka, Y.,Takahashi, S.,Sato, M.,Tsukihara, T.
Crystal structure of N-carbamyl-D-amino acid amidohydrolase with a novel catalytic framework common to amidohydrolases.
Structure Fold.Des., 8:729-737, 2000

PubMed Abstract: N-carbamyl-D-amino acid amidohydrolase (DCase) catalyzes the hydrolysis of N-carbamyl-D-amino acids to the corresponding D-amino acids, which are useful intermediates in the preparation of beta-lactam antibiotics. To understand the catalytic mechanism of N-carbamyl-D-amino acid hydrolysis, the substrate specificity and thermostability of the enzyme, we have determined the structure of DCase from Agrobacterium sp. strain KNK712.

PubMed: 10903946
DOI: 10.1016/S0969-2126(00)00160-X

Experimental method

X-RAY DIFFRACTION (1.7 Å)