Replacement of Asn233 in the substrate binding site of myosin by GLN increases the rate of ATP hydrolysis to the maximum actin activated rate

被引：0

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作者：

Li, XD

White, HD

Ikebe, R

Ikebe, M

机构：

[1] Univ Massachusetts, Sch Med, Worcester, MA 01655 USA

[2] Eastern Virginia Med Sch, Dept Physiol Sci, Norfolk, VA 23507 USA

来源：

BIOPHYSICAL JOURNAL | 1999年 / 76卷 / 01期

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D O I：

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中图分类号：

Q6 [生物物理学];

学科分类号：

071011 ;

摘要：

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页码：A49 / A49

页数：1

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[1] Binding of substrate at the effector site of pyrophosphatase increases the rate of its hydrolysis at the active site
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[2] Binding of substrate at the effector site of pyrophosphatase increases the rate of its hydrolysis at the active site
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Avaeva, S. M.
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[3] THE ACTIN-ACTIVATED ATPASES OF UNPHOSPHORYLATED AND PHOSPHORYLATED THYMUS MYOSIN HAVE THE SAME MAXIMUM RATE
WAGNER, PD
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[4] KINETIC-ANALYSIS OF PH-DEPENDENCE OF MAXIMUM RATE OF HYDROLYSIS OF CA-ATP BY MYOSIN
PETUSHKOVA, EV
SEMINA, TK
BIOCHEMISTRY-MOSCOW, 1977, 42 (12) : 1739 - 1747
[5] PHOSPHORYLATION OF THYMUS MYOSIN INCREASES ITS APPARENT AFFINITY FOR ACTIN BUT NOT ITS MAXIMUM ADENOSINE-TRIPHOSPHATASE RATE
WAGNER, PD
GEORGE, JN
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[6] DISTRIBUTION OF [O-18]PI SPECIES FROM [GAMMA-O-18]ATP HYDROLYSIS BY MYOSIN AND HEAVY-MEROMYOSIN - EVIDENCE FOR 2 KINDS OF MYOSIN-ACTIVE SITE DIFFERING IN THEIR RATE OF INTERMEDIATE OXYGEN-EXCHANGE
SHUKLA, KK
LEVY, HM
RAMIREZ, F
MARECEK, JF
MEYERSON, S
KUHN, ES
JOURNAL OF BIOLOGICAL CHEMISTRY, 1980, 255 (23) : 1344 - 1350