Download Metabolic Pathways by David Greenberg (Eds.) PDF

By David Greenberg (Eds.)

First released in 1954 lower than name: Chemical pathways of metabolism. First-2d versions cataloged lower than D. M. Greenberg

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By David Greenberg (Eds.)

First released in 1954 lower than name: Chemical pathways of metabolism. First-2d versions cataloged lower than D. M. Greenberg

Show description

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Detailed studies on the mechanism of this amination reaction have not been reported, but its superficial resemblance to the amination of XMP is evident. In the present case, one might anticipate that a transient 6-phospho-UTP or related intermediate might be formed by reaction with ATP; such an intermediate would then accept the NH 2 group derived either from glutamine or ammonia. 2. , formate, formaldehyde, and the ß-carbon of serine, were more effectively incorporated than was the methyl group of methionine (see 357).

The last component can then interact with external acceptors such as NAD or certain other oxidizing agents (335). Recent work by Taylor et al. (336,337) indicates that another type of dihydroorotate dehydrogenase occurs, at least in certain bacteria, which is more important in the biosynthesis of pyrimidines. These results suggest that nonparticulate enzymes such as the one described from Z. oroticum appear primarily in response to a need to degrade orotate. Under conditions of culture on glucose or glycerol, E.

HARTMAN 26 ADP lower the Km for AMP without affecting the maximum velocity, and convert the kinetic behavior to normal hyperbolic (165,169,170). GTP and GDP, as well as orthophosphate, antagonize the effect of the adenine nucleotides (165,171). Monovalent cations also activate the deaminase, and in the case of the one from the muscle, complete activation occurs at isotonic salt concentrations so that no further effect of nucleotide polyphosphates is observed (172). 6. DEAMINATION OF GMP TO IMP The enzyme, GMP reductase, catalyzes the reaction: GMP + NADPH + H + ->IMP + NADP+ + NH3 The examination of mutants of enteric bacteria lacking this enzyme clearly demonstrate its essential role in converting guanine compounds to the central metabolite, IMP (139).

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