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GABA transaminase 의 새로운 보조인자 유사체로서의 6 - Br - pyridoxal - 5 - phosphate
최수영,위세찬,김두식 ( Soo Young Choi,Sechan Wee,Doo Sik Kim ) 생화학분자생물학회 1989 BMB Reports Vol.22 No.2
6-Br-pyridoxal-5-phosphate, a new cofactor analog of pyridoxal-5-phosphate, was synthesized and purified homogeneously by organic and enzymatic methods. This cofactor analog binds to cofactor binding site of GABA transaminase. Resolved and reduced GABA transaminase restore the catalytic activity by 6-Br-PLP. These results indicate that the 6-Br-PLP remains covalently attached to the amino acid residue of the catalytic site and acts like natural cofactor.
Effect of fur on pyrC Gene Expression
Sangho Chai,Chang Kyu Song,Seong Kwun Kim,Jun Ho Park,Sechan Wee 한국미생물학회 2007 The journal of microbiology Vol.45 No.6
The promoter region of pyrC (dihydroorotase) gene of Escherichia coli was shown to have Fur protein binding properties by gel retardation assay. In vivo regulation of the pyrC expression was studied by measuring dihydroorotase activity and β-galactosidase level in the fur+ and fur- genetic background. The expression of chromosomal dihydroorotase activity and β-galactosidase activity of pyrC-lacZ fusion plasmid was repressed to about 30% and 17%, respectively in the fur+ strain compared to those in the fur- strain. Divalent ions such as Fe2+ and Zn2+ were not required for the repression. PyrC expression was also reduced to one half by 1 mM uracil. The effect of uracil was independent on the fur gene.
Catalytic and Structural Properties of Brain Glutamate Decarboxylase
Soo Young Choi,Su Jin Lee,Sang He Jang,Sechan Wee,Joon Ho Choe,Kil Soo Lee 생화학분자생물학회 1993 BMB Reports Vol.26 No.7
An homogeneous glutamate decarboxylase isolated from porcine brain contains 0.8 ㏖ of a tightly bound pyridoxal-5-phosphate per one mole enzyme dimer. Upon addition of exogeneous pyridoxal-5-P, the enzyme acquires maximum catalytic activity. The purified enzyme was deactivated by sulfhydryl reagents and mycotoxin patulin. Recovery from inhibition after the addition of dithiothreitol or 2-mercaptoetnanol suggests that critical sulfhydryl residues in the catalytic domain of the enzyme are connected with catalytic activity, and that the mycotoxin patulin reacts with these sulfhydryl residues of the enzyme.