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1
Amino acid sequence around lipoic acid residues in the pyruvate dehydrogenase multienzyme complex of Escherichia coli.大肠杆菌丙酮酸脱氢酶多酶复合体中硫辛酸残基周围的氨基酸序列。
Biochem J. 1980 Jun 1;187(3):905-8. doi: 10.1042/bj1870905.
2
Evidence for two lipoic acid residues per lipoate acetyltransferase chain in the pyruvate dehydrogenase multienzyme complex of Escherichia coli.大肠杆菌丙酮酸脱氢酶多酶复合物中每个硫辛酸乙酰转移酶链含有两个硫辛酸残基的证据。
Biochem J. 1976 Dec 1;159(3):677-82. doi: 10.1042/bj1590677.
3
Isolation and characterization of lipoylated and unlipoylated domains of the E2p subunit of the pyruvate dehydrogenase complex of Escherichia coli.大肠杆菌丙酮酸脱氢酶复合体E2p亚基脂酰化和非脂酰化结构域的分离与鉴定
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4
Three-dimensional structure of a lipoyl domain from the dihydrolipoyl acetyltransferase component of the pyruvate dehydrogenase multienzyme complex of Escherichia coli.大肠杆菌丙酮酸脱氢酶多酶复合体中二氢硫辛酰乙酰转移酶组分的硫辛酰结构域的三维结构。
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5
Polypeptide-chain stoicheiometry and lipoic acid content of the pyruvate dehydrogenase complex of Escherichia coli.
Biochem J. 1979 Jan 1;177(1):129-36. doi: 10.1042/bj1770129.
6
Lipoic acid content of dihydrolipoyl transacylases determined by isotope dilution analysis.通过同位素稀释分析法测定二氢硫辛酰转酰基酶的硫辛酸含量。
Biochem Biophys Res Commun. 1980 May 14;94(1):78-84. doi: 10.1016/s0006-291x(80)80190-2.
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Eur J Biochem. 1980 Dec;112(3):589-99.
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Bovine kidney pyruvate dehydrogenase complex. Isolation of the component enzymes after limited proteolysis with papain.
Eur J Biochem. 1980 Apr;105(2):371-9. doi: 10.1111/j.1432-1033.1980.tb04510.x.
9
Pyruvate dehydrogenase multienzyme complex of Escherichia coli: determination of the Mr of the lipoate acetyltransferase component.大肠杆菌丙酮酸脱氢酶多酶复合体：硫辛酰乙酰转移酶组分的相对分子质量测定
FEBS Lett. 1981 Oct 12;133(1):112-4. doi: 10.1016/0014-5793(81)80483-8.
10
Kinetic analysis of the role of lipoic acid residues in the pyruvate dehydrogenase multienzyme complex of Escherichia coli.硫辛酸残基在大肠杆菌丙酮酸脱氢酶多酶复合体中作用的动力学分析
Biochem J. 1980 May 1;187(2):393-401. doi: 10.1042/bj1870393.

引用本文的文献

1
Expression and lipoylation in Escherichia coli of the inner lipoyl domain of the E2 component of the human pyruvate dehydrogenase complex.人丙酮酸脱氢酶复合体E2组分内部硫辛酰结构域在大肠杆菌中的表达及硫辛酰化
Biochem J. 1993 Jan 1;289 ( Pt 1)(Pt 1):81-5. doi: 10.1042/bj2890081.
2
Limited proteolysis and proton n.m.r. spectroscopy of the 2-oxoglutarate dehydrogenase multienzyme complex of Escherichia coli.大肠杆菌2-氧代戊二酸脱氢酶多酶复合物的有限蛋白酶解和质子核磁共振光谱分析
Biochem J. 1981 Dec 1;199(3):733-40. doi: 10.1042/bj1990733.
3
The role of lipoic acid residues in the pyruvate dehydrogenase multienzyme complex of Escherichia coli.硫辛酸残基在大肠杆菌丙酮酸脱氢酶多酶复合体中的作用。
Biochem J. 1981 Dec 1;199(3):505-11. doi: 10.1042/bj1990505.
4
Repeating functional domains in the pyruvate dehydrogenase multienzyme complex of Escherichia coli.大肠杆菌丙酮酸脱氢酶多酶复合体中的重复功能结构域。
EMBO J. 1984 Jun;3(6):1315-9. doi: 10.1002/j.1460-2075.1984.tb01969.x.
5
Domain structure and 1H-n.m.r. spectroscopy of the pyruvate dehydrogenase complex of Bacillus stearothermophilus.嗜热脂肪芽孢杆菌丙酮酸脱氢酶复合体的结构域结构与一维核磁共振光谱分析
Biochem J. 1984 Jan 1;217(1):219-27. doi: 10.1042/bj2170219.
6
Limited proteolysis and sequence analysis of the 2-oxo acid dehydrogenase complexes from Escherichia coli. Cleavage sites and domains in the dihydrolipoamide acyltransferase components.大肠杆菌2-氧代酸脱氢酶复合物的有限蛋白酶解及序列分析。二氢硫辛酰胺酰基转移酶组分中的切割位点和结构域。
Biochem J. 1987 Mar 1;242(2):531-8. doi: 10.1042/bj2420531.
7
Primary structure around the lipoate-attachment site on the E2 component of bovine heart pyruvate dehydrogenase complex.牛心丙酮酸脱氢酶复合体E2组分上硫辛酸附着位点周围的一级结构。
Biochem J. 1987 Aug 1;245(3):919-22. doi: 10.1042/bj2450919.

本文引用的文献

1
The oxidation of ribonuclease with performic acid.用过甲酸氧化核糖核酸酶。
J Biol Chem. 1956 Apr;219(2):611-21.
2
The subunit molecular weights of the alpha-ketoacid dehydrogenase multienzyme complexes from E. coli.来自大肠杆菌的α-酮酸脱氢酶多酶复合物的亚基分子量。
FEBS Lett. 1971 Jun 2;15(1):8-12. doi: 10.1016/0014-5793(71)80066-2.
3
The subunit structure of the Escherichia coli K-12 pyruvate dehydrogenase complex. The dihydrolipoamide transacetylase component.
Eur J Biochem. 1971 May 28;20(2):169-78. doi: 10.1111/j.1432-1033.1971.tb01375.x.
4
The multienzyme alpha-keto acid dehydrogenase complexes.多酶α-酮酸脱氢酶复合体
Brookhaven Symp Biol. 1968 Jun;21(2):397-412.
5
Evidence for two lipoic acid residues per lipoate acetyltransferase chain in the pyruvate dehydrogenase multienzyme complex of Escherichia coli.大肠杆菌丙酮酸脱氢酶多酶复合物中每个硫辛酸乙酰转移酶链含有两个硫辛酸残基的证据。
Biochem J. 1976 Dec 1;159(3):677-82. doi: 10.1042/bj1590677.
6
Subunit structure of dihydrolipoyl transacetylase component of pyruvate dehydrogenase complex from Escherichia coli.来自大肠杆菌的丙酮酸脱氢酶复合体中二氢硫辛酰胺转乙酰酶组分的亚基结构。
Proc Natl Acad Sci U S A. 1979 Sep;76(9):4385-9. doi: 10.1073/pnas.76.9.4385.
7
Primary structure of the swinging arms of the pyruvate dehydrogenase complex of Escherichia coli.大肠杆菌丙酮酸脱氢酶复合体摆动臂的一级结构。
FEBS Lett. 1979 Sep 15;105(2):263-6. doi: 10.1016/0014-5793(79)80625-0.
8
Molecular weight and symmetry of the pyruvate dehydrogenase multienzyme complex of Escherichia coli.
J Mol Biol. 1979 Apr 25;129(4):603-17. doi: 10.1016/0022-2836(79)90471-6.
9
Limited proteolysis of the pyruvate dehydrogenase multienzyme complex of Escherichia coli.大肠杆菌丙酮酸脱氢酶多酶复合物的有限蛋白酶解
Eur J Biochem. 1979 Feb 15;94(1):119-26. doi: 10.1111/j.1432-1033.1979.tb12878.x.
10
Dihydrolipoamide transacetylase from Escherichia Coli: evidence for internal gene duplication.来自大肠杆菌的二氢硫辛酰胺转乙酰酶：内部基因重复的证据。
Biochem Biophys Res Commun. 1978 Sep 29;84(2):508-14. doi: 10.1016/0006-291x(78)90198-5.

大肠杆菌丙酮酸脱氢酶多酶复合体中硫辛酸残基周围的氨基酸序列。

Amino acid sequence around lipoic acid residues in the pyruvate dehydrogenase multienzyme complex of Escherichia coli.

作者信息

Hale G, Perham R N

出版信息

Biochem J. 1980 Jun 1;187(3):905-8. doi: 10.1042/bj1870905.

DOI:10.1042/bj1870905
PMID:6821375
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC1162478/
Abstract

Amino-acid sequences around two lipoic acid residues in the lipoate acetyltransferase component of the pyruvate dehydrogenase complex of Escherichia coli were investigated. A single amino acid sequence of 13 residues was found. A repeated amino acid sequence in the lipoate acetyltransferase chain might explain this result.

摘要

对大肠杆菌丙酮酸脱氢酶复合体中硫辛酸乙酰转移酶组分里两个硫辛酸残基周围的氨基酸序列进行了研究。发现了一段由13个残基组成的单一氨基酸序列。硫辛酸乙酰转移酶链中的重复氨基酸序列或许可以解释这一结果。