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Yeast phosphoglyceric acid mutase-modifying enzyme.

作者信息

Sasaki R, Sugimoto R, Chiba H

出版信息

Arch Biochem Biophys. 1966 Jul;115(1):53-61. doi: 10.1016/s0003-9861(66)81037-8.

DOI:10.1016/s0003-9861(66)81037-8
PMID:5966527
Abstract
摘要

相似文献

1
Yeast phosphoglyceric acid mutase-modifying enzyme.酵母磷酸甘油酸变位酶修饰酶
Arch Biochem Biophys. 1966 Jul;115(1):53-61. doi: 10.1016/s0003-9861(66)81037-8.
2
Studies on the active site of yeast phosphoglycerate mutase.酵母磷酸甘油酸变位酶活性位点的研究。
Biochim Biophys Acta. 1971 Mar 10;227(3):584-94. doi: 10.1016/0005-2744(71)90009-x.
3
Reversible urea denaturation of crystalline yeast phosphoglyceric acid mutase.
Arch Biochem Biophys. 1966 Feb;113(2):444-50. doi: 10.1016/0003-9861(66)90212-8.
4
[Properties of Chorismate-mutase from Saccharomyces cerexisiae S 288 C].[来自酿酒酵母S288C的分支酸变位酶的特性]
Hoppe Seylers Z Physiol Chem. 1970 Oct;351(10):1178-90.
5
The isolation and crystallization of yeast and rabbit liver triose phosphate isomerase and a comparative characterization with the rabbit muscle enzyme.酵母和兔肝磷酸丙糖异构酶的分离与结晶以及与兔肌肉酶的比较表征
Eur J Biochem. 1970 Jun;14(2):289-300. doi: 10.1111/j.1432-1033.1970.tb00289.x.
6
A preliminary x-ray crystallographic investigation of yeast phosphoglycerate mutase.酵母磷酸甘油酸变位酶的初步X射线晶体学研究。
J Mol Biol. 1971 Oct 14;61(1):257-9. doi: 10.1016/0022-2836(71)90222-1.
7
Studies on a role of the 2,3-diphosphoglycerate phosphatase activity in the yeast phosphoglycerate mutase reaction.关于2,3-二磷酸甘油酸磷酸酶活性在酵母磷酸甘油酸变位酶反应中作用的研究。
Biochim Biophys Acta. 1971 Mar 10;227(3):595-607. doi: 10.1016/0005-2744(71)90010-6.
8
Purification and properties of yeast invertase.酵母转化酶的纯化及性质
Biochemistry. 1967 Feb;6(2):468-75. doi: 10.1021/bi00854a015.
9
[Properties and amino acid composition of purified ATP: guanidinoacetate phosphotransferase].
Biochim Biophys Acta. 1968 Feb 19;154(2):305-14.
10
Nucleoside triphosphate-nucleoside diphosphate transphosphorylase (nucleoside diphosphokinase). II. Physical properties of the crystalline enzyme from brewers' yeast.
Biochemistry. 1967 Sep;6(9):2923-32. doi: 10.1021/bi00861a037.

引用本文的文献

1
Structural units important for activity of a novel-type phosphoserine phosphatase from Hydrogenobacter thermophilus TK-6 revealed by crystal structure analysis.通过晶体结构分析揭示了来自嗜氢菌 TK-6 的新型磷酸丝氨酸磷酸酶的活性所必需的结构单元。
J Biol Chem. 2013 Apr 19;288(16):11448-58. doi: 10.1074/jbc.M112.449561. Epub 2013 Mar 11.
2
Structural and functional analysis of Rv3214 from Mycobacterium tuberculosis, a protein with conflicting functional annotations, leads to its characterization as a phosphatase.对结核分枝杆菌Rv3214(一种功能注释存在冲突的蛋白质)进行结构和功能分析,结果表明它是一种磷酸酶。
J Bacteriol. 2006 May;188(10):3589-99. doi: 10.1128/JB.188.10.3589-3599.2006.
3
The role of the C-terminal region in phosphoglycerate mutase.
磷酸甘油酸变位酶中C末端区域的作用。
Biochem J. 1999 Jan 1;337 ( Pt 1)(Pt 1):89-95.
4
The amino acid sequence of the small monomeric phosphoglycerate mutase from the fission yeast Schizosaccharomyces pombe.来自裂殖酵母粟酒裂殖酵母的小单体磷酸甘油酸变位酶的氨基酸序列。
Biochem J. 1994 Feb 1;297 ( Pt 3)(Pt 3):603-8. doi: 10.1042/bj2970603.
5
The complete amino acid sequence of human erythrocyte diphosphoglycerate mutase.人红细胞二磷酸甘油酸变位酶的完整氨基酸序列。
EMBO J. 1983;2(7):1213-20. doi: 10.1002/j.1460-2075.1983.tb01569.x.
6
Alpha-isopropylmalate synthase from yeast: purification, kinetic studies, and effect of ligands on stability.酵母中的α-异丙基苹果酸合酶:纯化、动力学研究及配体对稳定性的影响。
J Bacteriol. 1972 Jun;110(3):1118-26. doi: 10.1128/jb.110.3.1118-1126.1972.
7
Properties of fructose 1,6-diphosphate aldolases from spores and vegetative cells of Bacillus cereus.蜡样芽孢杆菌孢子和营养细胞中1,6-二磷酸果糖醛缩酶的特性
J Bacteriol. 1969 Jun;98(3):1208-18. doi: 10.1128/jb.98.3.1208-1218.1969.
8
Molecular varieties of isozymes.同工酶的分子种类
Experientia. 1968 Oct 15;24(10):977-91. doi: 10.1007/BF02138698.
9
The bisphosphonomethyl analogue of 2,3-bisphosphoglycerate inhibits yeast but not wheat-germ phosphoglycerate mutase.2,3-二磷酸甘油酸的双膦酸甲酯类似物可抑制酵母磷酸甘油酸变位酶,但对小麦胚芽磷酸甘油酸变位酶无抑制作用。
Biochem J. 1987 Apr 1;243(1):301-4. doi: 10.1042/bj2430301.
10
Inactivation of rabbit muscle phosphoglycerate mutase by limited proteolysis with thermolysin.嗜热菌蛋白酶有限水解使兔肌肉磷酸甘油酸变位酶失活
Biochem J. 1985 Jul 1;229(1):167-71. doi: 10.1042/bj2290167.