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논문 기본 정보
- 자료유형
- 학술저널
- 저자정보
- 저널정보
- 한국미생물생명공학회 Journal of Microbiology and Biotechnology Journal of Microbiology and Biotechnology 제16권 제9호
- 발행연도
- 2006.1
- 수록면
- 1,434 - 1,440 (7page)
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초록· 키워드
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The stable anchorage of pyridoxal 5'-phosphate(PLP) in the active site of D-amino acid transaminase (D-AT)structure of D-AT revealed that Glu32 is one of the active sitegroups that may play a role in PLP binding. To prove the roleof Glu32 in PLP stability, we firstly checked the rate of thepotential rate-limiting step. The kinetic analysis showed thatthe rate of the α-deprotonation step reduced to 26-folds inE32A mutant enzyme. Spectral analyses of the reaction of D-AT with D-serine revealed that the E32A mutant enzymea quinonoid intermediate (E-Q). Finally, analysis of circulardichroism (CD) on the wild-type and E32A mutant enzymesshowed that the optical activity of PLP in the enzyme activesite was lost by the removal of the carboxylic group, provingthat Glu32 is inded involved in the cofactor anchorage. Theresults sugested that the electrostatic interaction networkthrough the groups from PLP, Glu32, His47, and Arg50,which was observed from the three-dimensional structure ofthe enzyme, plays a crucial role in the stable anchorage of thesubstrate complex.
#Transaminase
#quinonoid
#cofactor
#pyridoxal
#D-amino acidD-Amino acid transaminase
#D-AT
#EC 2.6.1.21) is apyridoxal 5'-phosphate
#PLP) dependent enzyme andcatalyzes the following transamination reaction betweenvarious D-amino acids and α-keto acids
#Transaminase
#quinonoid
#cofactor
#pyridoxal
#D-amino acidD-Amino acid transaminase
#D-AT
#EC 2.6.1.21) is apyridoxal 5'-phosphate
#PLP) dependent enzyme andcatalyzes the following transamination reaction betweenvarious D-amino acids and α-keto acids
목차
등록된 정보가 없습니다.
참고문헌 (21)
참고문헌 신청
Bae, H. S / 2002 / Application of a thermostable glutamate racemase from Bacillus sp. SK-1 for the production of Dphenylalanine in a multi-enzyme system / J. Mol. Catal. BEnz
Burkhard, P / 1998 / Three-dimensional structure of O-acetylserine sulfhydrylase from Salmonella typhimurium / J. Mol. Biol. 283 : 121 ~ 133
Futaki, S / 1990 / Substitution of glutamine for lysine at the pyridoxal phosphate binding site of bacterial Damino acid transaminase / J. Biol. Chem. 265
Gallagher, D. T / 1998 / Structure and control of pyridoxal phosphate dependent allosteric threonine deaminase / Structure 6 : 465 ~ 475
Hayashi, H / 1995 / Reaction of aspartate aminotransferase with L-erythro-3-hydroxyaspartate: Involvement of Tyr70 in stabilization of the catalytic intermediate / Biochemist
Burkhard, P / 1998 / Three-dimensional structure of O-acetylserine sulfhydrylase from Salmonella typhimurium / J. Mol. Biol. 283 : 121 ~ 133
Futaki, S / 1990 / Substitution of glutamine for lysine at the pyridoxal phosphate binding site of bacterial Damino acid transaminase / J. Biol. Chem. 265
Gallagher, D. T / 1998 / Structure and control of pyridoxal phosphate dependent allosteric threonine deaminase / Structure 6 : 465 ~ 475
Hayashi, H / 1995 / Reaction of aspartate aminotransferase with L-erythro-3-hydroxyaspartate: Involvement of Tyr70 in stabilization of the catalytic intermediate / Biochemist
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