Structure determination of the UDP-disaccharide fragment of cytoplasmic cofactor isolated from Methanobacterium thermoautotrophicum.
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.
Marsden
B J
BJ
National Research Council, Ottawa, Ontario, Canada.
Sauer
F D
FD
Blackwell
B A
BA
Kramer
J K
JK
D001685:Biological Factors; D002852:Chromatography, Ion Exchange; D019605:Euryarchaeota / Q000032:analysis*; D009682:Magnetic Resonance Spectroscopy; D013058:Mass Spectrometry; D014500:Uracil Nucleotides / Q000031:analogs & derivatives*; D014530:Uridine Diphosphate / Q000031:analogs & derivatives* / Q000302:isolation & purification
D001685:Biological Factors; D014500:Uracil Nucleotides; C059075:uridine 5'-(O-2-acetamido-2-deoxymannopyranuronosyl acid-(1--4)-2-acetamide-2-deoxyglucopyranosyl diphosphate); D014530:Uridine Diphosphate