Biotin in metabolism and its relationship to human disease

被引：107

作者：

Pacheco-Alvarez, D ^{[1
]}

Solórzano-Vargas, RS ^{[1
]}

Del Río, AL ^{[1
]}

机构：

[1] Univ Nacl Autonoma Mexico, Dept Mol Biol & Biotechnol, IIBM, CU, Mexico City 04510, DF, Mexico

来源：

ARCHIVES OF MEDICAL RESEARCH | 2002年 / 33卷 / 05期

关键词：

biotin; holocarboxylase synthetase; biotin deficiency; multiple carboxylase deficiency;

D O I：

10.1016/S0188-4409(02)00399-5

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：

Biotin, a water-soluble vitamin, is used as cofactor of enzymes involved in carboxylation reactions. In humans, there are five biotin-dependent carboxylases: propionyl-CoA carboxylase; methylcrotonyl-CoA carboxylase; pyruvate carboxylase, and two forms of acetylCoA carboxylase. These enzymes catalyze key reactions in gluconeogenesis, fatty acid metabolism, and amino acid catabolism; thus, biotin plays an essential role in maintaining metabolic homeostasis. In recent years, biotin has been associated with several diseases in humans. Some are related to enzyme deficiencies involved in biotin metabolism. However, not all biotin-responsive disorders can be explained based on the classical role of the vitamin in cell metabolism. Several groups have suggested that biotin may be involved in regulating transcription or protein expression of different proteins. Biotinylation of histones and triggering of transduction signaling cascades have been suggested as underlying mechanisms behind these non-classical biotin-deficiency manifestation in humans. (C) 2002 IMSS. Published by Elsevier Science Inc.

引用

页码：439 / 447

页数：9

共 95 条

[1] The subcellular localization of acetyl-CoA carboxylase 2 [J].

Abu-Elheiga, L ;

Brinkley, WR ;

Zhong, L ;

Chirala, SS ;

Woldegiorgis, G ;

Wakil, SJ .

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2000, 97 (04) :1444-1449

[2] HUMAN ACETYL-COA CARBOXYLASE - CHARACTERIZATION, MOLECULAR-CLONING, AND EVIDENCE FOR 2 ISOFORMS [J].

ABUELHEIGA, L ;

JAYAKUMAR, A ;

BALDINI, A ;

CHIRALA, SS ;

WAKIL, SJ .

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1995, 92 (09) :4011-4015

[3]

AbuElheiga L, 1997, J BIOL CHEM, V272, P10669

[4] 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

[5] ENZYME STUDIES IN COMBINED CARBOXYLASE DEFICIENCY [J].

BARTLETT, K ;

GHNEIM, HK ;

STIRK, JH ;

WASTELL, HJ ;

SHERRATT, HSA ;

LEONARD, JV .

ANNALS OF THE NEW YORK ACADEMY OF SCIENCES-SERIES, 1985, 447 (JUN) :235-251

[6]

BARTLETT K, 1976, LANCET, V2, P804

[7] The molecular basis of human 3-methylcrotonyl-CoA carboxylase deficiency [J].

Baumgartner, MR ;

Almashanu, S ;

Suormala, T ;

Obie, C ;

Cole, RN ;

Packman, S ;

Baumgartner, ER ;

Valle, D .

JOURNAL OF CLINICAL INVESTIGATION, 2001, 107 (04) :495-504

[8] The biotin domain peptide from the biotin carboxyl carrier protein of Escherichia coli acetyl-CoA carboxylase causes a marked increase in the catalytic efficiency of biotin carboxylase and carboxyltransferase relative to free biotin [J].

Blanchard, CZ ;

Chapman-Smith, A ;

Wallace, JC ;

Waldrop, GL .

JOURNAL OF BIOLOGICAL CHEMISTRY, 1999, 274 (45) :31767-31769

[9]

Borboni P, 1996, ACTA DIABETOL, V33, P154

[10]

BROWNER MF, 1989, J BIOL CHEM, V264, P12680

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