A COMPARISON OF THE ENZYMICALLY CATALYZED OXIDATION OF GLYCERALDEHYDE-3-PHOSPHATE AND LACTATE
作者： M.G. Rossmann
DOI: 10.1016/B978-0-12-691402-3.50006-8
关键词: Biochemistry 、 Lactate dehydrogenase 、 Branched-chain alpha-keto acid dehydrogenase complex 、 Cofactor 、 Chemistry 、 Glyceraldehyde 3-phosphate dehydrogenase 、 Dehydrogenase 、 Malate dehydrogenase 、 Glyceraldehyde 3-phosphate 、 Alcohol dehydrogenase 、 Stereochemistry
摘要: Publisher Summary This chapter presents a comparison of enzymically catalyzed oxidation glyceraldehyde-3-phosphate and lactate. Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) lactate (LDH) have similarity to alcohol in the nature their substrates, products cofactor. However, these enzymes do not require any metal such as zinc for catalysis. The negatively charged substrates are bound respective by providing positively environment. Small spatial changes, different isozymes, cause large differences rate constants. During binding cofactor substrate there conformational changes which orient position reactive groups. Chemical modification amino acids involved processes reduces or destroys activity. also structural similarities among dehydrogenases. subunit structures LDH, soluble malate (sHDH), liver (LADH) GAPDH dinucleotide domain common.
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