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

FEBS Letters

Milon, Alain²  Vorholt, Julia A¹  Saurel, Olivier²  Pomper, Barbara K¹ 

[1] Laboratoire de Biologie Moléculaire des Relations Plantes–Microorganismes, INRA/CNRS, P.O. Box 27, 31326 Castanet-Tolosan, France;Institut de Pharmacologie et de Biologie Structurale, 31077 Toulouse, France

关键词: Methylotrophic bacterium;    Tetrahydromethanopterin;    Methanofuran;    1H-nuclear magnetic resonance;    Amidohydrolase;    Ftr;    formyltransferase;    Fhc;    Ftr/hydrolase complex;    H4MPT;    tetrahydromethanopterin;    H4F;    tetrahydrofolate;    MFR;    methanofuran;    Mch;    methenyl-H4MPT cyclohydrolase;   

DOI  :  10.1016/S0014-5793(02)02962-9

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 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 Ftr 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.

【 授权许可】

Unknown