Bacterial trimethylamine dehydrogenase contains a covalently bound yellow coenzyme, the properties of which distinguish it from all known riboflavin, pyridoxine, and pteridine derivatives. A pure dodecapeptide containing the covalently linked coenzyme has been isolated from tryptic-chymotryptic digests. Treatment with aminopeptidase M converts it to a ninhydrin-positive aminoacyl coenzyme, whic...

The identity of the major cobamide in liver has not been satisfactorily established. Cyanocobalamin (vitamin B12, 5,6dimethylbenzimidazolylcobamide cyanide), which has been obtained in crystalline form with liver as a source material (1, 2), is certainly a very minor component of the cobalamins in liver. Analyses of liver concentrates, both by a paper chromatographicbioautographic method (3) an...

The enzymatic conversion of vitamin Ba to its coenzyme form has been described in cell-free systems derived from Propionibacterium shermanii (1) and from Clostridium tetanomorphum (2). The 5’-deoxyadenosyl moiety that replaces the cobalt-bound cyanide of cyanocobalamin during Blz coenzyme formation is derived from adenosine triphosphate (ATP) (3). In the present work, the fate of the phosphate ...

Methyl-coenzyme M reductase (MCR) catalyzes both the synthesis and anaerobic oxidation of methane (AOM). Its catalytic site contains Ni at core cofactor F430. The ion, in its low-valent Ni(I) state, lights fuse leading to homolysis C–S bond methyl-coenzyme (methyl-SCoM) generate a methyl radical, which abstracts hydrogen atom from coenzyme B (HSCoB) mixed disulfide CoMSSCoB. Direct reversal thi...

It was reported previously that coenzyme A contained pantothenic acid bound in such a manner as to make it unavailable in microbiological tests (1). A liberation of p;alanine on acid hydrolysis indicated early the presence of pantothenic acid, which was confirmed by chick assay (2). While the chick assay for pantothenic acid and the p-alanine assay by the yeast growth test yielded equivalent am...

Normal duck erythrocytes and erythrocytes infected with Plasmodium lopharae have all of the enzymes for coenzyme A biosynthesis, whereas parasites freed from their host cells have non. Since erythrocytefree cultivation of P. lophurae requires an exogenous source of coenzyme A, this parasite must obtain its coenzyme A entirely from the host cell during infection.