Clostridium tetanomorphum

Arthrobacter hjalinus Pacillus megaterium Butyribacterium rettgeri Clostridium sticklandii Clostridium tetanomorphum Clostridium thermoaceticum... 

In 1958 Barker (20) isolated a red, heat stable, light labile, cofactor which was required for the metabolism of glutamate in cell-extracts of Clostridium tetanomorphum. Subsequently this cofactor was crystallized. X-ray crystallography identified Barker s cofactor as the coenzyme form of Vitamin B12 (15, 21). 

Twarog, R. Wolfe, R.S. Role of butyryl phosphate in the energy metabolism of Clostridium tetanomorphum. J. Bacteriol., 86, 112-117 (1963)... 

Vitamin B12 (1) was first isolated in 1948. But it was not until 1958 that the biologically active form of this coenzyme was identified by H.A. Barker and his colleagues [4], who at that time were studying the metabolism of Clostridium tetanomorphum growing on glutamate. 

Holloway, D. E., and Marsh, E. N. G., 1994, Adenosylcobalamin-dependent glutamate mutase from Clostridium tetanomorphum. Overexpression in Escherichia coli, purification, and characterization of the recombinant enzyme. J. Biol. Chem. 269 20425920430. 

Tollinger, M., Konrat, R., Hilbert, B. H., Marsh, E. N. G., and Kr%outler, B., 1998, How aprotein prepares for Bij binding structure and dynamics of the Bi 2-binding subunit of glutamate mutase from Clostridium tetanomorphum. Structure 6 1021nl033. 

A variety of 3-substituted aspartic acids 7 can be prepared by stereospecific addition of ammonia to substituted fumaric acids 6 catalyzed by /(-methylaspartase (EC 4.3.1.2). The enzyme, which was first isolated from Clostridium tetanomorphum (ATCC 15920)42, aminates... 

For several years after the discovery of cobalamin its biochemical function remained a mystery, a major reason being the extreme sensitivity of the coenzymes to decomposition by light. Progress came after Barker and associates discovered that the initial step in the anaerobic fermentation of glutamate by Clostridium tetanomorphum is rearrangement to 3-methylaspar-... 

From the structure of precorrin-4 69 and its status as substrate for the CobM enzyme, clearly a methyltransferase from its sequence, the exact function of this enzyme could be deduced. In Clostridium tetanomorphum [106-108], Pr. shermanii [109] and Ps. denitrificans [88], the order of insertion of the various methyl groups into the corrin macrocycle, after the third one in precorrin-3 A 55, had been revealed by pulse labelling and this order was the same in all three. The fourth one was placed at position 17, then at 12 a followed by 1 and, finally, 5 and 15. Precorrin-4 69 shows the C-17 methyl group in place and Sect. 3.5 reported that the 12a-methyl of the corrin system is initially inserted at C-11. It is that C-11 methylation which is blocked by deletion of the cohM gene and hence CobM is the 11 -methyltransferase of Ps. denitrificans. 

Bear et al. have been using methylaspartate ammonia-lyase from Clostridium tetanomorphum to produce optically active pure precursors [3-methyl-, 3-ethyl and... 

S)-Citramalic acid (also shown below as 1029), the a-methyl analog of ( S)-malic acid, has been isolated from a variety of natural sources. It can be produced microbially by incubation of mesaconic acid with an extract from Clostridium tetanomorphum cells [220]. 

Occurrence F. I is formed as oxidation product of precorrin 1 on isolation from vitamin B 2-produc-ing bacteria, e.g., Propionibacterium shermanii and Clostridium tetanomorphum. Precorrin 1 is the tetra-hydro form of F. I and has been identified as the biosynthetic intermediate directly following uroporphyrinogen III (see uroporphyrins) in the biosynthetic pathway leading to vitamin B12. 

Arigoni D, Imfeld M (1979) Factor I ex Clostridium tetanomorphum Proof of Structure and Relationship to Vitamin B12 Biosynthesis. In Zagalak B, Friedrich W (eds) Vitamin B12. de Gruyter, Berlin, New York, p 315... 

Methylaspartase from Clostridium tetanomorphum catalyses the stereospecific addition of ammonia to mesaconic acid (23) to yield (2S,3S)-3-methylaspartic acid (24). The latter can then be converted to the isosteric L-valine analogue (2/ , 3/l)-3-bromobutyrine (25) (Scheme 5.21). 

In a study of differential labeling of the allosteric site for 5 -ADP binding in the L-threonine dehydratase of Clostridium tetanomorphum, six reagents were compared for their ability to produce a loss in ADP binding in the absence or in the presence of ADP as a protective ligand. 

The nature of the Bir-like compounds synthesized by Clostridium tetanomorphum (Hendlin, 1953) is unknown. Clostridia abound in most intestinal microfloras. 

Wachsman, J. T. and Barker, H. A. (1955) Tracer experiments on glutamate fermentation by Clostridium tetanomorphum. J. Biol. Chem. 217, 695-702. 

Ljungdahl, L., Irion, E. and Wood, H. G. (1965) Total synthesis of acetate from CO,. I. Co-methyl-cobyric acid and Co-(methyl)-5-methoxybenzimidazolyl-cobamide as intermediates with Clostridium tetanomorphum. Biochem. 4,2771-2780. 

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