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- W164037127 abstract "This chapter presents a comparison of enzymically catalyzed oxidation of glyceraldehyde-3-phosphate and lactate. Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and lactate dehydrogenase (LDH) have a similarity to alcohol dehydrogenase in the nature of their substrates, products and cofactor. However, these enzymes do not require any metal such as zinc for catalysis. The negatively charged substrates are bound to their respective enzymes by providing a positively charged environment. Small spatial changes, as in different lactate dehydrogenase isozymes, cause large differences in rate constants. During the binding of cofactor and substrate to these enzymes there are conformational changes which orient and position the reactive groups. Chemical modification of the amino acids involved in these processes reduces or destroys activity. The chapter also presents structural similarities among dehydrogenases. The subunit structures of LDH, soluble malate dehydrogenase (sHDH), liver alcohol dehydrogenase (LADH) and GAPDH have a dinucleotide binding domain in common." @default.
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- W164037127 date "1977-01-01" @default.
- W164037127 modified "2023-09-26" @default.
- W164037127 title "A COMPARISON OF THE ENZYMICALLY CATALYZED OXIDATION OF GLYCERALDEHYDE-3-PHOSPHATE AND LACTATE" @default.
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- W164037127 doi "https://doi.org/10.1016/b978-0-12-691402-3.50006-8" @default.
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