Roles of Amino Acid Residues Surrounding Phosphorylation Site 1 of Branched-chain -Ketoacid Dehydrogenase (BCKDH) in Catalysis and Phosphorylation Site Recognition by BCKDH Kinase (*)
Roles of Amino Acid Residues Surrounding Phosphorylation Site 1 of Branched-chain -Ketoacid Dehydrogenase (BCKDH) in Catalysis and Phosphorylation Site Recognition by BCKDH Kinase (*)
复制标题
支链酮酸脱氢酶 (BCKDH) 磷酸化位点 1 周围的氨基酸残基在 BCKDH 激酶的催化和磷酸化位点识别中的作用 (*)
DOI：
--
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发表时间：
1995
影响因子：
4.8
通讯作者：
R. Harris
中科院分区：
文献类型：
--
作者：
J. Hawes;R. Schnepf;A. Jenkins;Y. Shimomura;K. M. Popov;R. Harris
Branched-chain α-ketoacid dehydrogenase is regulated by reversible phosphorylation of serine 293 (site 1) on the E1α subunit. Alanine-scanning mutagenesis was used to examine the roles of residues surrounding serine 293 in catalysis by the dehydrogenase and in substrate recognition by branched-chain α-ketoacid dehydrogenase kinase. Alanine substitution of serine 293 resulted in a 10-fold increased K for α-ketoisovalerate, a less increased (2.8-fold) Kfor α-ketoisocaproate, but no change in V or the K for thiamine pyrophosphate. Alanine substitutions of arginine 288, histidine 292, and aspartate 296, residues highly conserved among α-ketoacid dehydrogenases, resulted in inactive enzymes. Each of the inactive E1 mutants bound to the E2 core subunit with equal affinity as wild-type E1, and each produced circular dichroism spectra identical to that of wild-type E1. Two mutations, H292A and S293E, abolished the ability of E1 apoenzyme to reconstitute with thiamine pyrophosphate. Each alanine-substituted E1 was phosphorylated at site 1 by branched-chain α-ketoacid dehydrogenase kinase with similar rates, with the exception of the R288A mutant, which displayed no detectable phosphorylation. Thiamine pyrophosphate inhibited the phosphorylation of all mutant enzymes with the exception of H292A, the mutant E1 that did not bind thiamine pyrophosphate.
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单价阳离子和无机磷酸盐改变支链 α-酮酸脱氢酶激酶活性和抑制剂敏感性。
影响因子：
3.9
作者：
Shimomura,Y;Kuntz,MJ;Suzuki,M;Ozawa,T;Harris,RA
通讯作者：
Harris,RA
支链α-酮酸脱氢酶的调节和枫糖浆尿病的分子基础的阐明。
DOI：
10.1016/0065-2571(90)90021-s
发表时间：
1990
期刊：
Advances in enzyme regulation
影响因子：
--
作者：
Harris,RA;Zhang,B;Goodwin,GW;Kuntz,MJ;Shimomura,Y;Rougraff,P;Dexter,P;Zhao,Y;Gibson,R;Crabb,DW
通讯作者：
Crabb,DW
牛丙酮酸脱氢酶活性位点必需半胱氨酸残基的鉴定。
DOI：
--
发表时间：
1993
期刊：
The Journal of biological chemistry
影响因子：
--
作者：
Ali,MS;Roche,TE;Patel,MS
通讯作者：
Patel,MS
影响因子：
3.9
作者：
PAXTON, R;HARRIS, RA
通讯作者：
HARRIS, RA
5-磷酸吡哆醛对哺乳动物丙酮酸脱氢酶的活性位点进行修饰。
影响因子：
2.9
作者：
Stepp,LR;Reed,LJ
通讯作者：
Reed,LJ