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By S. N. Ananchenko (Eds.)

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By S. N. Ananchenko (Eds.)

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Read or Download Frontiers of Bioorganic Chemistry and Molecular Biology. Proceedings of the International Symposium on Frontiers of Bioorganic Chemistry and Molecular Biology, Moscow and Tashkent, USSR, 25 September–2 October 1978 PDF

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Additional info for Frontiers of Bioorganic Chemistry and Molecular Biology. Proceedings of the International Symposium on Frontiers of Bioorganic Chemistry and Molecular Biology, Moscow and Tashkent, USSR, 25 September–2 October 1978

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7. The sequence around arginine-8l (*) reactive with 1,2-cyclohexanedione in the NADP enzyme, and for comparison, the similar sequences in the other two types of glutamate dehydrogenases. For the NAD-specific enzyme of Neurospora, the situation is strikingly different (22). With iodoacetate or iodoacetamide there is no reaction whatsoever; however, one sulfhydryl group reacts with a variety of other reagents. Hydroxymercuribenzoate produces almost complete inactivation whereas formation of the cyano derivative has only a slight effect on the ac­ tivity.

Therefore, the secondary interactions c o n ­ tribute to stabilizing the transition state, chiefly by decreasing i t s energy, but display only a minor effect on the probability of i t s formation. TABLE 1. u. u. 6 N02 ZVal-Phe-AlaAPM 1 1 N02 ZLeu-Val-Phe-AlaAPM NOg I APM - v» -aminopropylmorpholine 1 31 Catalysis by Proteolytic Enzymes It has been accepted so far that the transition state is stabilized either due to realization in it of new interactions between the enzyme and a sub­ strate which are not observed in the ground state, or because a strain arising in the ground state when the substrate is bound are eliminated in the transition state (Ref.

Blocking these sulfhydryl groups has no effect on the activity of the enzyme although the stability of the enzyme is decreased. From this finding,it is evident that sulfhydryl groups play no catalytic role in this enzyme. BOVINE -Lys-Gly-Gly-Ile-Arg}Tyr-Ser-Thr-AspJ- Val-Ser4Val90 9k 101 NADP-GDH -Lys-Gly-GlyjLeu{Arg}Leu-His-Pro Ser-Val|Asn-Leu~ 81 11 " "S3 NAD-GDH -ArgiGly-Gly-Ile-Arg[lle-Val-Lys}-Ser}-Arg}Ser|LysC501 C597 C^90 Fig. 7. The sequence around arginine-8l (*) reactive with 1,2-cyclohexanedione in the NADP enzyme, and for comparison, the similar sequences in the other two types of glutamate dehydrogenases.

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