1sch

From Proteopedia

Revision as of 13:59, 30 October 2007

PEANUT PEROXIDASE

Overview

BACKGROUND. Peroxidases catalyze a wide variety of peroxide-dependent, oxidations. Based on sequence alignments, heme peroxidases have been, divided into three classes. Crystal structures are available for, peroxidases of classes I and II, but until now no structure has been, determined for class III, the classical extracellular plant peroxidases., RESULTS. The crystal structure of peanut peroxidase has been solved to 2.7, A resolution. The helical fold is similar to that of known peroxidase, structures. The 294-residue polypeptide chain is accompanied by a heme and, two calcium ions, and there is some evidence of glycosylation., CONCLUSIONS. This is the first complete structure of a class III, peroxidase and as such should serve as a model for other class III enzymes, including the ... [(full description)]

About this Structure

1SCH is a [Single protein] structure of sequence from [Arachis hypogaea] with NAG, CA and HEM as [ligands]. Active as [Peroxidase], with EC number [1.11.1.7]. Structure known Active Sites: ADC, ADH, APC, APH, BDC, BDH, BPC and BPH. Full crystallographic information is available from [OCA].

Reference

The crystal structure of peanut peroxidase., Schuller DJ, Ban N, Huystee RB, McPherson A, Poulos TL, Structure. 1996 Mar 15;4(3):311-21. PMID:8805539

Page seeded by OCA on Tue Oct 30 16:03:52 2007