Biochemistry, Volume 2, Second Edition: The Chemical by David E. Metzler

By David E. Metzler

During this e-book you discover classical biochemistry, and many it. not like such a lot different biochemistry textbooks which waft clear of the subject and pass an increasing number of into mobile biology, immunology and so on, Metzler concentrates at the imperative subject matters of biochemistry, the enzymes and their mechanisms. there is not any different publication the place one is prone to locate detailled infomation at the structure-function relation of virtually any enzyme (with the single draw back of getting merely black-and-white photographs, even for structures). This e-book is, besides the fact that, to be taken care of with warning: it isn't protecting the subjects of such a lot biochem novices classes (or is delivering an excessive amount of details that's approximately to crush green readers, respectively). nonetheless, it is going to be an unavoidable table connection with any biochemist who cares approximately enzymes and should be hugely invaluable not less than so long as the former version from 1977.

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Another route to lactate is through addition of water to acrylyl-CoA, the product of step a of Fig. 17-3. The water molecule adds in the “wrong way,” the OH – ion going to the α carbon instead of the β (Eq. 17-8). An enzyme with an active site similar to that of histidine ammonia-lyase (Eq. 14-48) could 948 Chapter 17. The Organization of Metabolism 1 3 H3C COO– 2 CH2 Propionate ATP O H3C Catabolism of “odd” and branched fatty acids and of isoleucine CoA-SH C S CH2 CoA b Propionyl-CoA CO2 ATP O ADP + Pi H3C a C C Biotin-enzyme Acyl-CoA oxidase S O (S)-Methylmalonyl-CoA C S CH Racemase CoA Acrylyl-CoA O H2O H3C C C O S CH2 HO CoA d 3-Hydroxypropionyl-CoA O NAD+ Hydrolase –OOC CoA-SH O H COO– CH2 C CH2 O 3-Hydroxypropionate CH3 CoA CoA GDP + Pi GTP –OOC Succinate C CH2 S β Oxidation CoA Malonyl-CoA CO2 NAD+ O S O Malonic semialdehyde CO2 S –2[H] CH2 CoA-SH –2[H] C CH2 Succinyl-CoA CH2 COO– C H2 C C NAD+ H O Vitamin B12 coenzyme c H2O HO CoA H (R)-Methylmalonyl-CoA C CH2 S –OOC Methylmalonyl-CoA pathway H2C Modified β Oxidation pathway CoA COO– H Oxaloacetate Pyruvate Biosynthesis CO2 C S CoA CO2 Acetyl-CoA Figure 17-3 Catabolism of propionate and propionyl-CoA.

A. (1990) J. Biol. Chem. 265, 16705 – 16708 958 Chapter 17. 98,99 For example, bacteria subsisting on succinate as a carbon source must oxidize it for energy as well as convert some of it to carbohydrates, lipids, and other materials. Complete combustion of any citric acid cycle intermediate can be accomplished by conversion to malate followed by oxidation of malate to oxaloacetate (Eq. 17-10, step a) and decarboxylation (β cleavage) to pyruvate, or (Eq. 17-10, step b) oxidation and decarboxylation of malate by the malic enzyme (Eq.

The Methylmalonyl-CoA Pathway of Propionate Utilization Despite the simplicity and logic of the β oxidation pathway of propionate metabolism, higher animals use primarily the more complex methylmalonyl-CoA pathway (Fig. 17-3, step b). This is one of the two processes in higher animals presently known to depend upon vitamin B12. This vitamin has never been found in higher plants, nor does the methylmalonyl pathway occur in plants. The pathway (Fig. 17-3) begins with the biotin- and ATP-dependent carboxylation of propionyl-CoA.

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