Crystallization and preliminary crystallographic characterization of recombinant L-methionine-alpha-deamino-gamma-mercaptomethane lyase (methioninase) | Health & Environmental Research Online (HERO)

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Citation
Tags

HERO ID

2304044

Reference Type

Journal Article

Title

Crystallization and preliminary crystallographic characterization of recombinant L-methionine-alpha-deamino-gamma-mercaptomethane lyase (methioninase)

Author(s)

Sridhar, V; Xu, MX; Han, QH; Sun, XH; Tan, YY; Hoffman, RM; Prasad, GS

Year

2000

Is Peer Reviewed?

Yes

Journal

Acta Crystallographica. Section D: Biological Crystallography
ISSN: 0907-4449

Volume

Issue

Pt 12

Page Numbers

1665-1667

Language

English

PMID

11092940

DOI

10.1107/S0907444900013251

Web of Science Id

WOS:000165509100024

Abstract

L-Methionine-alpha-deamino-gamma-mercaptomethane lyase (rMETase) is involved in the alpha,gamma-elimination of methionine to alpha-ketobutyrate, methanethiol and ammonia. The reaction catalyzed by rMETase reduces the methionine concentration of methionine-dependent tumor cells, arresting their growth. Towards the goal of developing rMETase into an effective antitumor therapeutic and also to understand the catalytic mechanism of this enzyme, rMETase from Pseudomonas putida has been expressed, purified and crystallized. The crystals belong to space group P2(1)2(1)2 and diffract X-rays to at least 2.68 A resolution at 100 K using synchrotron radiation. The unit cell has parameters a = 152.8, b = 154.6, c = 80.8 A and contains four molecules in the asymmetric unit.