Enzyme Promiscuity in the Hormone-sensitive Lipase Family of Proteins

被引：10

作者：

Giuseppe, Manco ^{[1
]}

Luigia, Merone ^{[1
]}

Elena, Porzio ^{[1
]}

Yan, Feng ^{[2
,3
]}

Luigi, Mandrich ^{[1
]}

机构：

[1] CNR, Ist Biochim Prot, I-80131 Naples, Italy

[2] Shanghai Jiao Tong Univ, Key Lab MOE Microbial Metab, Shanghai 200240, Peoples R China

[3] Shanghai Jiao Tong Univ, Sch Life Sci & Biotechnol, Shanghai 200240, Peoples R China

来源：

PROTEIN AND PEPTIDE LETTERS | 2012年 / 19卷 / 02期

关键词：

Promiscuity; alpha/beta hydrolase fold; hormone-sensitive lipase family; ALPHA/BETA-HYDROLASE-FOLD; AEROPYRUM-PERNIX K1; ALICYCLOBACILLUS-ACIDOCALDARIUS; THERMOPHILIC ESTERASE; CATALYTIC PROMISCUITY; ACYLAMINOACYL PEPTIDASE; SUBSTRATE-SPECIFICITY; SEQUENCE SIMILARITY; DIRECTED EVOLUTION; REACTION-MECHANISM;

D O I：

10.2174/092986612799080400

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：

The number of enzymes endowed with the capacity to catalyse other reactions than the main, physiological one, a feature that has been called promiscuity, is increasing at a fast pace. Promiscuity is a highly pervasive phenomenon that is present at each level of life complexity. For enzymes, promiscuity encompasses interesting aspects related to their physiological role, evolution and biotechnological applications. Herein, at first we will describe some general aspects of enzyme promiscuity and then we will report some examples from the alpha/beta hydrolase superfamily of proteins, with particular emphasis to the hormone-sensitive lipase family.

引用

页码：144 / 154

页数：11

共 86 条

[1] The latent promiscuity of newly identified microbial lactonases is linked to a recently diverged phosphotriesterase
Afriat, Livnat
Roodveldt, Cintia
Manco, Giuseppe
Tawfik, Dan S.
[J]. BIOCHEMISTRY, 2006, 45 (46) : 13677 - 13686
[2] The 'evolvability' of promiscuous protein functions
Aharoni, A
Gaidukov, L
Khersonsky, O
Gould, SM
Roodveldt, C
Tawfik, DS
[J]. NATURE GENETICS, 2005, 37 (01) : 73 - 76
[3] Bacterial lipolytic enzymes: classification and properties
Arpigny, JL
Jaeger, KE
[J]. BIOCHEMICAL JOURNAL, 1999, 343 : 177 - 183
[4] Understanding enzyme superfamilies - Chemistry as the fundamental determinant in the evolution of new catalytic activities
Babbitt, PC
Gerlt, JA
[J]. JOURNAL OF BIOLOGICAL CHEMISTRY, 1997, 272 (49) : 30591 - 30594
[5] What makes an enzyme promiscuous?
Babtie, Ann
Tokuriki, Nobuhiko
Hollfelder, Florian
[J]. CURRENT OPINION IN CHEMICAL BIOLOGY, 2010, 14 (02) : 200 - 207
[6] Molecular basis of perhydrolase activity in serine hydrolases
Bernhardt, P
Halt, K
Kazlauskas, RJ
[J]. ANGEWANDTE CHEMIE-INTERNATIONAL EDITION, 2005, 44 (18) : 2742 - 2746
[7] In the light of directed evolution: Pathways of adaptive protein evolution
Bloom, Jesse D.
Arnold, Frances H.
[J]. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2009, 106 : 9995 - 10000
[8] A hierarchical approach to protein molecular evolution
Bogarad, LD
Deem, MW
[J]. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1999, 96 (06) : 2591 - 2595
[9] Enzyme-like proteins by computational design
Bolon, DN
Mayo, SL
[J]. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2001, 98 (25) : 14274 - 14279
[10] Catalytic promiscuity in biocatalysis: Using old enzymes to form new bonds and follow new pathways
Bornscheuer, UT
Kazlauskas, RJ
[J]. ANGEWANDTE CHEMIE-INTERNATIONAL EDITION, 2004, 43 (45) : 6032 - 6040

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