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오리의 Uropygial Gland 에서 분리한 Glucose - 6 - phosphate Dehydrogenase Isozyme 의 Kinetic 특성
김우택,서경훈,김유삼 ( Woo Taek Kim,Yyong Hoon Seo,Yu Sam Kim ) 생화학분자생물학회 1984 BMB Reports Vol.17 No.4
One isozyme of glucose-6-phosphate dehydrogenase with pI of 6.6 was purified from the uropygial gland of Peking duck and its kinetic properties were examined. The reaction by the enzyme followed ordered bi-bi reaction mechanism which was also detected in the reaction by the purified liver G6-PD of the same duck. Km values to G-6-P and NADP+ for the gland G6-PD were 101 μM and 4. 41 μM, respectively. And for the liver enzyme, Km to G-6-P was 76.92 μM and to NADP+ was 9.09 μM. Km to substrate analogs, galactose-6-phosphate and 2-deoxy-D-glucose-6-phosphate, for the gland enzyme were 6.7×10³ ACM and 3.65×10³ μM, respectively. NAD+ was not used as a coenzyme by the gland even though its concentration was raised up to 9. 7 mM. NADPH, a product of the enzyme reaction, was competitive inhibitor to NADP+ with Ki of 42.5 μM for the gland enzyme. On the other hand, that Ki of the liver enzyme was 25 μM. For the gland enzyme, glucosamine-6-phosphate was an uncompetitive inhibitor to NADP+ and ATP was a noncompetitive one. These results, the high substrate affinity and high Ki value of NADPH for the gland enzyme, indirectly indicated that the gland G-6-PD was well designed enzyme for the active and continuous production of surface-lipids in the uropygial gland.
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