兔肌醛缩酶催化磷酸二羟丙酮、D-果糖1,6-二磷酸和D-果糖1-磷酸中C-1位前手性氢的质子交换。 - Suppr | 超能文献

Proton exchange of the pro-S hydrogen at C-1 in dihydroxyacetone phosphate, D-fructose 1,6-bisphosphate and D-fructose 1-phosphate catalysed by rabbit-muscle aldolase.

作者信息

Lowe G, Pratt R F

出版信息

Eur J Biochem. 1976 Jun 15;66(1):95-104. doi: 10.1111/j.1432-1033.1976.tb10429.x.

DOI:10.1111/j.1432-1033.1976.tb10429.x

Abstract

摘要

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Proton exchange of the pro-S hydrogen at C-1 in dihydroxyacetone phosphate, D-fructose 1,6-bisphosphate and D-fructose 1-phosphate catalysed by rabbit-muscle aldolase.兔肌醛缩酶催化磷酸二羟丙酮、D-果糖1,6-二磷酸和D-果糖1-磷酸中C-1位前手性氢的质子交换。

Eur J Biochem. 1976 Jun 15;66(1):95-104. doi: 10.1111/j.1432-1033.1976.tb10429.x.

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The proton exchange of the pro-S hydrogen atom at C-1 in dihydroxyacetone phosphate and D-fructose 1,6-bisphosphate catalysed by class-I and class-II aldolases.I类和II类醛缩酶催化磷酸二羟丙酮和D-果糖1,6-二磷酸中C-1位前手性氢原子的质子交换。

Biochem J. 1978 Jun 1;171(3):539-42. doi: 10.1042/bj1710539.

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Fructose 1,6-bisphosphate aldolase from rabbit muscle. The isomerization of the enzyme-dihydroxyacetone phosphate complex.来自兔肌肉的果糖1,6 - 二磷酸醛缩酶。酶 - 磷酸二羟丙酮复合物的异构化作用

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A functional arginine residue in rabbit-muscle aldolase.兔肌肉醛缩酶中的一个功能性精氨酸残基。

Eur J Biochem. 1976 Nov 15;70(2):517-22. doi: 10.1111/j.1432-1033.1976.tb11043.x.

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Anomeric specificity of fructosediphosphate aldolase E.C.4.1.2.13 from rabbit muscle.来自兔肌肉的果糖二磷酸醛缩酶（E.C.4.1.2.13）的异头特异性

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Fructose-1,6-bisphosphate aldolase from rabbit muscle: different catalytic behavior of the dihydroxyacetone phosphate binding sites at low temperature.兔肌肉中的果糖-1,6-二磷酸醛缩酶：低温下磷酸二羟丙酮结合位点的不同催化行为。

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Fructose-bisphosphate aldolase from rabbit muscle. A thermodynamic study on the formation of the enzyme-dihydroxyacetone phosphate complex.来自兔肌肉的果糖二磷酸醛缩酶。关于酶-磷酸二羟丙酮复合物形成的热力学研究。

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The proton exchange of the pro-S hydrogen atom at C-1 in dihydroxyacetone phosphate and D-fructose 1,6-bisphosphate catalysed by class-I and class-II aldolases.I类和II类醛缩酶催化磷酸二羟丙酮和D-果糖1,6-二磷酸中C-1位前手性氢原子的质子交换。

Biochem J. 1978 Jun 1;171(3):539-42. doi: 10.1042/bj1710539.