Publisher Summary This chapter discusses the lactate dehydrogenase. Lactic acid is the end product of anaerobic glycolysis in muscle tissue has been known for all of this century. Cell-free extracts able to catalyze the oxidation of lactate to pyruvate. The five different permutations of two different polypeptide chains readily explained the electrophoretic patterns. The distribution of these two polypeptide chains was dependent on whether the extract originated in aerobic tissue, such as heart or in anaerobic tissue as in skeletal muscle. The NAD + binding structure found in L-lactate dehydrogenase (LDH) occurs frequently in other dehydrogenases and other proteins. In LDH the problem of catalysis is presented in stark simplicity. The complications of metal ions, linked substrate phosphorylation, or of ammonia uptake are absent. LDH is the only simpler dehydrogenase where both structure and sequence are known at present. The concept of multiple molecular forms of LDH has stimulated many investigations into the nature, function, and control of isozymes. There are only two major structural genes and there is a complex variety of other LDH genes, which can be expressed in some tissues at certain stages of development.

4 Lactate Dehydrogenase

http://www.jbc.org/content/239/6/1753.full.pdf

The Comparative Enzymology of Lactic Dehydrogenases I. PROPERTIES OF THE CRYSTALLINE BEEF AND CHICKEN ENZYMES

Negative cooperativity has been observed in CTP synthetase, an allosteric enzyme which contains a regulatory site. Thus, the same enzyme exhibits negative cooperativity for GTP (an effector) and glutamine (a substrate) and positive cooperativity for ATP and UTP (both substrates). In the process of the delineation of these phenomena, diagnostic procedures for negative cooperativity were developed. Application of these procedures to other enzymes indicates that negative cooperativity is a characteristic of many of them. These findings add strong support for the sequential model of subunit interactions which postulates that ligand-induced conformational changes are responsible for regulatory and cooperative phenomena in enzymes.

https://www.pnas.org/content/pnas/62/4/1121.full.pdf

Negative cooperativity in regulatory enzymes

The sequence of 13.9 kilobases (kb) of the 17.1-kb mitochondrial genome of Mytilus edulis has been determined, and the arrangement of all genes has been deduced. Mytilus mitochondrial DNA (mtDNA) contains 37 genes, all of which are transcribed from the same DNA strand. The gene content of Mytilus is typically metazoan in that it includes genes for large and small ribosomal RNAs, for a complete set of transfer RNAs and for 12 proteins. The protein genes encode the cytochrome b apoenzyme, cytochrome c oxidase (CO) subunits I-III, NADH dehydrogenase (ND) subunits 1-6 and 4L, and ATP synthetase (ATPase) subunit 6. No gene for ATPase subunit 8 could be found. The reading frames for the ND1, COI, and COIII genes contain long extensions relative to those genes in other metazoan mtDNAs. There are 23 tRNA genes, one more than previously found in any metazoan mtDNA. The additional tRNA appears to specify methionine, making Mytilus mtDNA unique in having two tRNA(Met) genes. Five lengthy unassigned intergenic sequences are present, four of which vary in length from 79 to 119 nucleotides and the largest of which is 1.2 kb. The base compositions of these are unremarkable and do not differ significantly from that of the remainder of the mtDNA. The arrangement of genes in Mytilus mtDNA is remarkably unlike that found in any other known metazoan mtDNA.

https://www.genetics.org/content/genetics/131/2/397.full.pdf

A novel mitochondrial genome organization for the blue mussel, Mytilus edulis.

http://science.sciencemag.org/content/sci/184/4132/28.full.pdf

Enzyme Polymorphism and Metabolism

Immunochemical and kinetic properties of anionic and cationic glutamic-oxaloacetic transaminases separated from human heart and human liver.

Purification and properties of human heart lactic dehydrogenase.

Reactions of Human Tissue Lactic Dehydrogenases with Antisera to Human Heart and Liver Lactic Dehydrogenases

Reactions of lactic dehydrogenase from various rabbit organs with antirabbit muscle lactic dehydrogenase.

Comparison of the actions of human brain, liver, and heart lactic dehydrogenase variants on nucleotide analogues and on substrate analogues in the absence and in the presence of oxalate and oxamate.

J.S. Nisselbaum

Papers

Immunochemical and kinetic properties of anionic and cationic glutamic-oxaloacetic transaminases separated from human heart and human liver.

Purification and properties of human heart lactic dehydrogenase.

Reactions of Human Tissue Lactic Dehydrogenases with Antisera to Human Heart and Liver Lactic Dehydrogenases

Reactions of lactic dehydrogenase from various rabbit organs with antirabbit muscle lactic dehydrogenase.

Comparison of the actions of human brain, liver, and heart lactic dehydrogenase variants on nucleotide analogues and on substrate analogues in the absence and in the presence of oxalate and oxamate.