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Histidine residues lactate dehydrogenase

The chemical modifications of cysteine sulfhydryl, histidine imidazole and arginine residues in lactate dehydrogenase lead to a total loss of enzymatic... [Pg.226]

The constancy of Ae.nad/Ae.nadh at pH 6.0-8.5 for other dehydrogenases in Table IV, notably the heart lactate dehydrogenases, means that a proton is released stoichiometrically in the reduction of E NAD to E NADH by substrate, just as in the overall reaction [Eq. (11)]. A histidine residue as proton source and sink was first suggested by Schwert et al. 56,67) and can now be identified with the single essential histidine per subunit 168) in the pig heart enzyme and histidine-195 in the dogfish enzyme. The constancy of Ae nad/Ae.nadh shows that the... [Pg.45]

See other pages where Histidine residues lactate dehydrogenase is mentioned: [Pg.300]    [Pg.347]    [Pg.259]    [Pg.341]    [Pg.200]    [Pg.347]    [Pg.87]    [Pg.1224]   
See also in sourсe #XX -- [ Pg.45 , Pg.199 , Pg.205 , Pg.208 , Pg.210 , Pg.221 , Pg.243 , Pg.245 , Pg.249 , Pg.251 , Pg.259 ]



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Dehydrogenases lactate dehydrogenase

Histidine residues

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