1erz

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1erz.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1erz.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1erz| PDB=1erz | SCENE= }}
{{STRUCTURE_1erz| PDB=1erz | SCENE= }}
-
'''CRYSTAL STRUCTURE OF N-CARBAMYL-D-AMINO ACID AMIDOHYDROLASE WITH A NOVEL CATALYTIC FRAMEWORK COMMON TO AMIDOHYDROLASES'''
+
===CRYSTAL STRUCTURE OF N-CARBAMYL-D-AMINO ACID AMIDOHYDROLASE WITH A NOVEL CATALYTIC FRAMEWORK COMMON TO AMIDOHYDROLASES===
-
==Overview==
+
<!--
-
BACKGROUND: 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. RESULTS: The crystal structure of DCase has been determined to 1.7 A resolution. The enzyme forms a homotetramer and each monomer consists of a variant of the alpha + beta fold. The topology of the enzyme comprises a sandwich of parallel beta sheets surrounded by two layers of alpha helices, this topology has not been observed in other amidohydrolases such as the N-terminal nucleophile (Ntn) hydrolases. CONCLUSIONS: The catalytic center could be identified and consists of Glu46, Lys126 and Cys171. Cys171 was found to be the catalytic nucleophile, and its nucleophilic character appeared to be increased through general-base activation by Glu46. DCase shows only weak sequence similarity with a family of amidohydrolases, including beta-alanine synthase, aliphatic amidases and nitrilases, but might share highly conserved residues in a novel framework, which could provide a possible explanation for the catalytic mechanism for this family of enzymes.
+
The line below this paragraph, {{ABSTRACT_PUBMED_10903946}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 10903946 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_10903946}}
==About this Structure==
==About this Structure==
Line 35: Line 39:
[[Category: Yamashita, E.]]
[[Category: Yamashita, E.]]
[[Category: Four-layer sandwich]]
[[Category: Four-layer sandwich]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 15:27:04 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 01:47:05 2008''

Revision as of 22:47, 30 June 2008

Image:1erz.png

Template:STRUCTURE 1erz

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

Template:ABSTRACT PUBMED 10903946

About this Structure

1ERZ is a Single protein structure of sequence from Agrobacterium sp.. Full crystallographic information is available from OCA.

Reference

Crystal structure of N-carbamyl-D-amino acid amidohydrolase with a novel catalytic framework common to amidohydrolases., Nakai T, Hasegawa T, Yamashita E, Yamamoto M, Kumasaka T, Ueki T, Nanba H, Ikenaka Y, Takahashi S, Sato M, Tsukihara T, Structure. 2000 Jul 15;8(7):729-37. PMID:10903946

Page seeded by OCA on Tue Jul 1 01:47:05 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1erz"
Personal tools