Biotin synthase is catalytic in vivo, but catalysis engenders destruction of the protein

被引:49
作者
Choi-Rhee, E
Cronan, JE [1 ]
机构
[1] Univ Illinois, Dept Microbiol, Urbana, IL 61801 USA
[2] Univ Illinois, Dept Biochem, Urbana, IL 61801 USA
来源
CHEMISTRY & BIOLOGY | 2005年 / 12卷 / 04期
关键词
D O I
10.1016/j.chembiol.2005.02.006
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
Biotin synthase is responsible for the synthesis of biotin from dethlobiotin and sulfur. Although the name of the protein implies that it functions as an enzyme, it has been consistently reported that biotin synthase produces < 1 molecule of biotin per molecule of protein in vitro. Moreover, the source of the biotin sulfur atom has been reported to be the [2Fe-2S] center of the protein. Biotin synthase has therefore been designated as a substrate or reactant rather than an enzyme. We report in vivo experiments demonstrating that biotin synthase is catalytic but that catalysis puts the protein at risk of proteolytic destruction.
引用
收藏
页码:461 / 468
页数:8
相关论文
共 41 条
[1]   Structure of the biotinyl domain of acetyl-coenzyme A carboxylase determined by MAD phasing [J].
Athappilly, FK ;
Hendrickson, WA .
STRUCTURE, 1995, 3 (12) :1407-1419
[2]   THE BIRA GENE OF ESCHERICHIA-COLI ENCODES A BIOTIN HOLOENZYME SYNTHETASE [J].
BARKER, DF ;
CAMPBELL, AM .
JOURNAL OF MOLECULAR BIOLOGY, 1981, 146 (04) :451-467
[3]   GENETIC AND BIOCHEMICAL-CHARACTERIZATION OF THE BIRA GENE AND ITS PRODUCT - EVIDENCE FOR A DIRECT ROLE OF BIOTIN HOLOENZYME SYNTHETASE IN REPRESSION OF THE BIOTIN OPERON IN ESCHERICHIA-COLI [J].
BARKER, DF ;
CAMPBELL, AM .
JOURNAL OF MOLECULAR BIOLOGY, 1981, 146 (04) :469-492
[4]   Crystal structure of biotin synthase, an S-adenosylmethionine-dependent radical enzyme [J].
Berkovitch, F ;
Nicolet, Y ;
Wan, JT ;
Jarrett, JT ;
Drennan, CL .
SCIENCE, 2004, 303 (5654) :76-79
[5]   BIOTIN SYNTHASE FROM ESCHERICHIA-COLI, AN INVESTIGATION OF THE LOW-MOLECULAR-WEIGHT AND PROTEIN-COMPONENTS REQUIRED FOR ACTIVITY IN-VITRO [J].
BIRCH, OM ;
FUHRMANN, M ;
SHAW, NM .
JOURNAL OF BIOLOGICAL CHEMISTRY, 1995, 270 (32) :19158-19165
[6]   Fate of the (2Fe-2S)2+ cluster of Escherichia coli biotin synthase during reaction:: A Mossbauer characterization [J].
Bui, BTS ;
Benda, R ;
Schünemann, V ;
Florentin, D ;
Trautwein, AX ;
Marquet, A .
BIOCHEMISTRY, 2003, 42 (29) :8791-8798
[7]   Biotin synthase mechanism:: on the origin of sulphur [J].
Bui, BTS ;
Florentin, D ;
Fournier, F ;
Ploux, O ;
Méjean, A ;
Marquet, A .
FEBS LETTERS, 1998, 440 (1-2) :226-230
[8]   Covalent modification of an exposed surface turn alters the global conformation of the biotin carrier domain of Escherichia coli acetyl-CoA carboxylase [J].
ChapmanSmith, A ;
Forbes, BE ;
Wallace, JC ;
Cronan, JE .
JOURNAL OF BIOLOGICAL CHEMISTRY, 1997, 272 (41) :26017-26022
[9]   EXPRESSION, BIOTINYLATION AND PURIFICATION OF A BIOTIN-DOMAIN PEPTIDE FROM THE BIOTIN CARBOXY CARRIER PROTEIN OF ESCHERICHIA-COLI ACETYL-COA CARBOXYLASE [J].
CHAPMANSMITH, A ;
TURNER, DL ;
CRONAN, JE ;
MORRIS, TW ;
WALLACE, JC .
BIOCHEMICAL JOURNAL, 1994, 302 :881-887
[10]   Promiscuous protein biotinylation by Escherichia coli biotin protein ligase [J].
Choi-Rhee, E ;
Schulman, H ;
Cronan, JE .
PROTEIN SCIENCE, 2004, 13 (11) :3043-3050