Generation of formate by the formyltransferase/hydrolase complex (Fhc) from Methylobacterium extorquens AM1

被引：45

作者：

Pomper, BK

Saurel, O

Milon, A

Vorholt, JA

机构：

[1] INRA, CNRS, Lab Biol Mol Relat Plantes Microorganismes, F-31326 Castanet Tolosan, France

[2] Max Planck Inst Terr Mikrobiol, D-35043 Marburg, Germany

[3] Inst Pharmacol & Biol Struct, F-31077 Toulouse, France

来源：

FEBS LETTERS | 2002年 / 523卷 / 1-3期

关键词：

methylotrophic bacterium; tetrahydromethanopterin; methanofuran; H-1-nuclear magnetic resonance; amidohydrolase;

D O I：

10.1016/S0014-5793(02)02962-9

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Methylobacterium extorquens AM1 possesses a formyltransferase (Ftr) complex that is essential for growth in the presence of methanol and involved in formaldehyde oxidation to CO2. One of the subunits of the complex carries the catalytic site for transfer of the formyl group from tetrahydromethanopterin to methanofuran (MFR). We now found via nuclear magnetic resonance-based studies that the Fir complex also catalyzes the hydrolysis of formyl-MFR and generates formate. The enzyme was therefore renamed Ftr/hydrolase complex (Fhc). FhcA shares a sequence pattern with amidohydrolases and is assumed to be the catalytic site where the hydrolysis takes place. (C) 2002 Federation of European Biochemical Societies. Published by Elsevier Science B.V. All rights reserved.

引用

页码：133 / 137

页数：5

共 22 条

[21] Novel formaldehyde-activating enzyme in Methylobacterium extorquens AM1 required for growth on methanol [J].