Regulation of peptide bond cis/trans isomerization by enzyme catalysis and its implication in physiological processes
被引:197
作者:
Fischer, G
论文数: 0引用数: 0
h-index: 0
机构:
Max Planck Res Unit Enzymol Prot Folding, D-06120 Halle An Der Saale, GermanyMax Planck Res Unit Enzymol Prot Folding, D-06120 Halle An Der Saale, Germany
Fischer, G
[1
]
Aumüller, T
论文数: 0引用数: 0
h-index: 0
机构:
Max Planck Res Unit Enzymol Prot Folding, D-06120 Halle An Der Saale, GermanyMax Planck Res Unit Enzymol Prot Folding, D-06120 Halle An Der Saale, Germany
Aumüller, T
[1
]
机构:
[1] Max Planck Res Unit Enzymol Prot Folding, D-06120 Halle An Der Saale, Germany
来源:
REVIEWS OF PHYSIOLOGY, BIOCHEMISTRY AND PHARMACOLOGY, VOL 148
|
2004年
/
148卷
关键词:
D O I:
10.1007/s10254-003-0011-3
中图分类号:
Q5 [生物化学];
Q7 [分子生物学];
学科分类号:
071010 ;
081704 ;
摘要:
In some cases, the slow rotational movement underlying peptide bond cis/trans isomerizations is found to control the biological activity of proteins. Peptide bond cis/trans isomerases as cyclophilins, Fk506-binding proteins, parvulins, and bacterial hsp70 generally assist in the interconversion of the polypeptide substrate cis/trans isomers, and rate acceleration is the dominating mechanism of action in cells. We present evidence disputing the hypothesis that some of the molecular properties of these proteins play an auxiliary role in enzyme function.