Structure determination of the UDP-disaccharide fragment of cytoplasmic cofactor isolated from Methanobacterium thermoautotrophicum.

Abstract:

:The methylcoenzyme M methylreductase reaction has an absolute requirement for 7-mercaptoheptanoylthreonine phosphate or component B, which is the active component of the intact molecule previously referred to as cytoplasmic cofactor. A hydrolytic fragment of cytoplasmic cofactor has been purified and identified as uridine 5'-(O-2-acetamido-2-deoxy-beta-manno-pyranuronosyl acid (1----4)-2-acetamido-2-deoxy-alpha-glucopyranosyl diphosphate) by high resolution NMR and fast atom bombardment mass spectro-metry. It is postulated that UDP-disaccharide may function to anchor 7-mercaptoheptanoyl threonine phosphate at the active site of the methyl-reductase enzyme complex.

authors

Marsden BJ,Sauer FD,Blackwell BA,Kramer JK

doi

10.1016/0006-291x(89)92266-3

subject

Has Abstract

pub_date

1989-03-31 00:00:00

pages

1404-10

issue

3

eissn

0006-291X

issn

1090-2104

pii

0006-291X(89)92266-3

journal_volume

159

pub_type

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