ALLOSTERIC EFFECT OF TETRAHYDROBIOPTERIN COFACTORS ON TYROSINE-HYDROXYLASE ACTIVITY

被引：19

作者：

MINAMI, M

TAKAHASHI, T

MARUYAMA, W

TAKAHASHI, A

NAGATSU, T

NAOI, M

机构：

[1] NAGOYA INST TECHNOL,DEPT BIOSCI,SHOWA KU,NAGOYA,AICHI 466,JAPAN

[2] NAGOYA UNIV,SCH MED,DEPT NEUROL,NAGOYA,AICHI 466,JAPAN

[3] KONAN WOMENS COLL,DEPT FOOD & NUTR,KOBE,JAPAN

[4] FUJITA HLTH UNIV,INST COMPREHENS MED SCI,DIV MOLEC GENET 2 E NEUROCHEM,AICHI,JAPAN

来源：

LIFE SCIENCES | 1992年 / 50卷 / 01期

关键词：

D O I：

10.1016/0024-3205(92)90192-R

中图分类号：

R-3 [医学研究方法]; R3 [基础医学];

学科分类号：

1001 ;

摘要：

Allostery of tyrosine hydroxylase was found by kinetical studies of partially purified tyrosine hydroxylase from clonal rat pheochromocytoma PC 12h cells. Postitive cooperativity toward the cofactors, (6R-L-erythro-5,6,7,8-tetrahydrobiopterin [(6R)BH4] and (6S)-L-erythro-5,6,7,8-tetrahydrobiopterin [(6S)BH4], was observed. It is indicated that biopterin might be the regulatory factor of the enzyme polymers, which changes the affinity for the cofactor itself. Moreover, the stereochemical structure of (6R)BH4, the naturally-occurring cofactor, took an important role on the kinetical properties of the enzyme in concern with L-tyrosine.

引用

页码：15 / 20

页数：6

共 20 条

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[2]

GOLDSTEIN M, 1984, CATECHOLAMINES BASIC, P189

[3]

ITO T, 1988, BIOGENIC AMINES, V5, P489

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