Literature DB >> 14760735

Lipase-specific foldases.

Frank Rosenau1, Jan Tommassen, Karl-Erich Jaeger.   

Abstract

Lipases represent the most important class of enzymes used in biotechnology. Many bacteria produce and secrete lipases but the enzymes originating from Pseudomonas and Burkholderia species seem to be particularly useful for a wide variety of different biocatalytic applications. These enzymes are usually encoded in an operon together with a second gene which codes for a lipase-specific foldase, Lif, which is necessary to obtain enzymatically active lipase. A detailed analysis based on amino acid homology has suggested the classification of Lif proteins into four different families and also revealed the presence of a conserved motif, Rx1x2FDY(F/C)L(S/T)A. Recent experimental evidence suggests that Lifs are so-called steric chaperones, which exert their physiological function by lowering energetic barriers during the folding of their cognate lipases, thereby providing essential steric information needed to fold lipases into their enzymatically active conformation.

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Year:  2004        PMID: 14760735     DOI: 10.1002/cbic.200300761

Source DB:  PubMed          Journal:  Chembiochem        ISSN: 1439-4227            Impact factor:   3.164


  15 in total

1.  Crystallization and crystal manipulation of a steric chaperone in complex with its lipase substrate.

Authors:  Kris Pauwels; Remy Loris; Guy Vandenbussche; Jean Marie Ruysschaert; Lode Wyns; Patrick Van Gelder
Journal:  Acta Crystallogr Sect F Struct Biol Cryst Commun       Date:  2005-07-30

2.  Pseudomonas 2007.

Authors:  Joanna B Goldberg; Robert E W Hancock; Rebecca E Parales; Joyce Loper; Pierre Cornelis
Journal:  J Bacteriol       Date:  2007-12-28       Impact factor: 3.490

3.  The structure of Acinetobacter-secreted protease CpaA complexed with its chaperone CpaB reveals a novel mode of a T2SS chaperone-substrate interaction.

Authors:  Darya V Urusova; Rachel L Kinsella; Nichole D Salinas; M Florencia Haurat; Mario F Feldman; Niraj H Tolia
Journal:  J Biol Chem       Date:  2019-07-18       Impact factor: 5.157

4.  Components of the E. coli envelope are affected by and can react to protein over-production in the cytoplasm.

Authors:  Riccardo Villa; Marina Lotti; Pietro Gatti-Lafranconi
Journal:  Microb Cell Fact       Date:  2009-06-05       Impact factor: 5.328

5.  Hexadecane and Tween 80 stimulate lipase production in Burkholderia glumae by different mechanisms.

Authors:  Bouke K H L Boekema; Anke Beselin; Michael Breuer; Bernhard Hauer; Margot Koster; Frank Rosenau; Karl-Erich Jaeger; Jan Tommassen
Journal:  Appl Environ Microbiol       Date:  2007-04-27       Impact factor: 4.792

6.  Cloning and expression of gene, and activation of an organic solvent-stable lipase from Pseudomonas aeruginosa LST-03.

Authors:  Hiroyasu Ogino; Yoshikazu Katou; Rieko Akagi; Takashi Mimitsuka; Shinichi Hiroshima; Yuichi Gemba; Noriyuki Doukyu; Masahiro Yasuda; Kosaku Ishimi; Haruo Ishikawa
Journal:  Extremophiles       Date:  2007-07-27       Impact factor: 2.395

7.  Evolution of Subfamily I.1 Lipases in Pseudomonas aeruginosa.

Authors:  Zhenghong Zhang; Xuehong Zhang
Journal:  Curr Microbiol       Date:  2021-07-19       Impact factor: 2.188

8.  Enhanced Triacylglycerol Metabolism Contributes to Efficient Oil Utilization and High-Level Production of Salinomycin in Streptomyces albus ZD11.

Authors:  Han Li; Jiaxiu Wei; Jianxin Dong; Yudong Li; Yongquan Li; Yinghu Chen; Wenjun Guan
Journal:  Appl Environ Microbiol       Date:  2020-08-03       Impact factor: 4.792

9.  Defining the interaction of the protease CpaA with its type II secretion chaperone CpaB and its contribution to virulence in Acinetobacter species.

Authors:  Rachel L Kinsella; Juvenal Lopez; Lauren D Palmer; Nichole D Salinas; Eric P Skaar; Niraj H Tolia; Mario F Feldman
Journal:  J Biol Chem       Date:  2017-10-05       Impact factor: 5.157

10.  In vivo functional expression of a screened P. aeruginosa chaperone-dependent lipase in E. coli.

Authors:  Xiangping Wu; Pengyong You; Erzheng Su; Jingjing Xu; Bei Gao; Dongzhi Wei
Journal:  BMC Biotechnol       Date:  2012-09-06       Impact factor: 2.563

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