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.
journal_name
Biochem Biophys Res Communjournal_title
Biochemical and biophysical research communicationsauthors
Marsden BJ,Sauer FD,Blackwell BA,Kramer JKdoi
10.1016/0006-291x(89)92266-3subject
Has Abstractpub_date
1989-03-31 00:00:00pages
1404-10issue
3eissn
0006-291Xissn
1090-2104pii
0006-291X(89)92266-3journal_volume
159pub_type
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