Folding of barstar C40A/C82A/P27A and catalysis of the peptidyl-prolyl cis/trans isomerization by human cytosolic cyclophilin (Cyp18)

被引：33

作者：

Golbik, R

Fischer, G

Fersht, AR

机构：

[1] Univ Halle Wittenberg, Inst Biochem, Abt Enzymol, D-06120 Halle, Germany

[2] Max Planck Gesell Forderung Wissensch EV, Forsch Stelle Enzymol Prot Faltung, D-06120 Halle, Germany

[3] MRC, Ctr Prot Engn, Cambridge CB2 2QH, England

来源：

PROTEIN SCIENCE | 1999年 / 8卷 / 07期

关键词：

barstar; cyclophilin; enzymology; kinetics; peptidyl-prolyl cis trans isomerase; protein folding; thermodynamics;

D O I：

10.1110/ps.8.7.1505

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：

Refolding of b*C40A/C82A/P27A is comprised of several kinetically detectable folding phases. The slowest phase in refolding originates from trans --> cis isomerization of the Tyr47-Pro48 peptide bond being in cis conformation in the native state. This refolding phase can be accelerated by the peptidyl-prolyl cis/trans isomerase human cytosolic cyclophilin (Cyp18) with a k(cat)/K-M of 254,000 M-1 s(-1). The fast refolding phase is not influenced by the enzyme.

引用

收藏

页码：1505 / 1514

页数：10

相关论文

共 60 条

[41] Folding of tryptophan mutants of barstar: Evidence for an initial hydrophobic collapse on the folding pathway [J].

Nath, U ;

Udgaonkar, JB .

BIOCHEMISTRY, 1997, 36 (28) :8602-8610

[42] The folding pathway of a protein at high resolution from microseconds to seconds [J].

Nolting, B ;

Golbik, R ;

Neira, JL ;

SolerGonzalez, AS ;

Schreiber, G ;

Fersht, AR .

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1997, 94 (03) :826-830

[43] SUBMILLISECOND EVENTS IN PROTEIN-FOLDING [J].

NOLTING, B ;

GOLBIK, R ;

FERSHT, AR .

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1995, 92 (23) :10668-10672

[44] CRYSTALLIZATION AND MOLECULAR PACKING ANALYSIS OF BARSTAR CRYSTALS [J].

RAGHUNATHAN, V ;

KHURANA, S ;

GUPTA, V ;

KHURANA, R ;

UDGAONKAR, JB ;

SALUNKE, DM .

JOURNAL OF MOLECULAR BIOLOGY, 1994, 243 (03) :533-536

[45] Intramolecular assistance of cis/trans isomerization of the histidine-proline moiety [J].

Reimer, U ;

ElMokdad, N ;

Schutkowski, M ;

Fischer, G .

BIOCHEMISTRY, 1997, 36 (45) :13802-13808

[46] UNFOLDING FREE-ENERGY CHANGES DETERMINED BY THE LINEAR EXTRAPOLATION METHOD .1. UNFOLDING OF PHENYLMETHANESULFONYL ALPHA-CHYMOTRYPSIN USING DIFFERENT DENATURANTS [J].

SANTORO, MM ;

BOLEN, DW .

BIOCHEMISTRY, 1988, 27 (21) :8063-8068

[47] PROLYL ISOMERASE - ENZYMATIC CATALYSIS OF SLOW PROTEIN-FOLDING REACTIONS [J].

SCHMID, FX .

ANNUAL REVIEW OF BIOPHYSICS AND BIOMOLECULAR STRUCTURE, 1993, 22 :123-143

[48] ACID CATALYSIS OF FORMATION OF SLOW-FOLDING SPECIES OF RNASE-A - EVIDENCE THAT REACTION IS PROLINE ISOMERIZATION [J].

SCHMID, FX ;

BALDWIN, RL .

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1978, 75 (10) :4764-4768

[49] PROLYL ISOMERASES - ROLE IN PROTEIN-FOLDING [J].

SCHMID, FX ;

MAYR, LM ;

MUCKE, M ;

SCHONBRUNNER, ER .

ADVANCES IN PROTEIN CHEMISTRY, VOL 44, 1993, 44 :25-66

[50] MECHANISM OF FOLDING OF RIBONUCLEASE-A - SLOW REFOLDING IS A SEQUENTIAL REACTION VIA STRUCTURAL INTERMEDIATES [J].

SCHMID, FX .

BIOCHEMISTRY, 1983, 22 (20) :4690-4696

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