Identification of the gene encoding esterase, a homolog of hormone-sensitive lipase, from an oil-degrading bacterium, strain HD-1.

Identification of the gene encoding esterase, a homolog of hormone-sensitive lipase, from an oil-degrading bacterium, strain HD-1. Research Abstract Details 

Research Abstract Table of Contents

Jump to the:

Identification of the gene encoding esterase, a homolog of hormone-sensitive lipase, from an oil-degrading bacterium, strain HD-1. Abstract Text:

S Mizuguchi,K Amada,M Haruki,T Imanaka,M Morikawa,S Kanaya,

The gene encoding an esterase (HDE) was cloned from an oil-degrading bacterium, strain HD-1. HDE is a member of the hormone-sensitive lipase family and composed of 317 amino acid residues with a molecular weight of 33,633. The HDE-encoding gene was expressed in Escherichia coli, and the recombinant protein was purified and characterized. Amino acid sequence analysis indicated that the methionine residue was removed from its NH(2)-terminus. The good agreement of the molecular weights estimated by SDS-PAGE (35,000) and gel filtration (38,000) suggests that it acts in a monomeric form. HDE showed hydrolytic activity towards p-nitrophenyl esters of fatty acids with an acyl chain length of 2 to 14 and tributyrin, whereas it showed little hydrolytic activity towards p-nitrophenyl oleate (C(18)), tricaprylin and triolein. Determination of the kinetic parameters for the hydrolyses of the p-nitrophenyl substrates from C(2) to C(14) indicated that HDE shows a relatively broad substrate specificity. However, comparison of the k(cat)/K(m) values indicated that the C(10)-C(14) substrates are the most preferred ones. Such a preference for substrates with long acyl chains may be a characteristic of HDE.

Identification of the gene encoding esterase, a homolog of hormone-sensitive lipase, from an oil-degrading bacterium, strain HD-1. Publishing Authors By Initials

S Mizuguchi,K Amada,M Haruki,T Imanaka,M Morikawa,S Kanaya,

For similar biochemical phenomena, metabolism, and nutrition: biochemical phenomena: substrate specificity research abstracts see: biochemical phenomena, metabolism, and nutrition: biochemical phenomena: substrate specificity research

PUBMED ID PMID:

MEDLINE DATE:

Identification of the gene encoding esterase, a homolog of hormone-sensitive lipase, from an oil-degrading bacterium, strain HD-1. Journal Published:

PUBLICATION TYPE: Research Support, Non-U.S. Gov

Journal: Journal of biochemistry

VOLUME: 126

Page Numbers: 731-7

Journal Abbreviation: J. Biochem.

ISSN: 0021-924X

DAY: 19

MONTH: Oct

YEAR: 1999

Identification of the gene encoding esterase, a homolog of hormone-sensitive lipase, from an oil-degrading bacterium, strain HD-1. Information

Number of References:

LANGUAGE: eng

NlmUniqueID: 376600

Identification of the gene encoding esterase, a homolog of hormone-sensitive lipase, from an oil-degrading bacterium, strain HD-1. Keywords Mesh Terms:

KEYWORDS: Substrate Specificity

MESH TERMS: genetics

Chemical & Substance for Abstract: Identification of the gene encoding esterase, a homolog of hormone-sensitive lipase, from an oil-degrading bacterium, strain HD-1. Information

Substance Name: Sterol Esterase

Registry Number: EC 3.1.1.13

Grant and Affiliation Information for Identification of the gene encoding esterase, a homolog of hormone-sensitive lipase, from an oil-degrading bacterium, strain HD-1.

AFFILIATION: Department of Material and Life Science, Graduate School of Engineering, Osaka University, Osaka, 565-0871, Japan.

Country: JAPAN

AGENCY:

GRANT:

ACRONYM:

MEDLINETA: J Biochem

REFSOURCE:

DATABASENAME:

ACCESSION NUMBER: AB029896

Number Hits: 0

Identification of the gene encoding esterase, a homolog of hormone-sensitive lipase, from an oil-degrading bacterium, strain HD-1 Related Publications

• A neural network approach to a Bayesian statistical decision problem.
• Characterization of ribonuclease HII from Escherichia coli overproduced in a soluble form.
• Crystal structure of a family I.3 lipase from Pseudomonas sp. MIS38 in a closed conformation.
• Crystal structure of highly thermostable glycerol kinase from a hyperthermophilic archaeon in a dimeric form.
• Crystal structure of type 1 ribonuclease H from hyperthermophilic archaeon Sulfolobus tokodaii: role of arginine 118 and C-terminal anchoring.
• Effect of the disease-causing mutations identified in human ribonuclease (RNase) H2 on the activities and stabilities of yeast RNase H2 and archaeal RNase HII.
• Four new crystal structures of Tk-subtilisin in unautoprocessed, autoprocessed and mature forms: insight into structural changes during maturation.
• Highly extended conformation of polyelectrolytes incorporated into hybrid threadlike micelles studied by small angle neutron scattering.
• Hydrophobic effect on the stability and folding of a hyperthermophilic protein.
• Identification of the gene encoding esterase, a homolog of hormone-sensitive lipase, from an oil-degrading bacterium, strain HD-1.
• Metabolic profiling using Fourier-transform ion-cyclotron-resonance mass spectrometry.
• Metabolomics approach for determining growth-specific metabolites based on Fourier transform ion cyclotron resonance mass spectrometry.
• Mutational and structural-based analyses of the osmolyte effect on protein stability.
• Osmolyte effect on the stability and folding of a hyperthermophilic protein.
• Remarkable stabilization of a psychrotrophic RNase HI by a combination of thermostabilizing mutations identified by the suppressor mutation method.
• Requirement of left-handed glycine residue for high stability of the Tk-subtilisin propeptide as revealed by mutational and crystallographic analyses.
• Restorative yoga in adults with metabolic syndrome: a randomized, controlled pilot trial.
• Review: Orlistat, sibutramine, and rimonabant reduce weight in overweight and obese persons.
• Structural and thermodynamic analyses of Escherichia coli RNase HI variant with quintuple thermostabilizing mutations.
• [COLOR REACTION WITH XANTHYDROL. V. MECHANISMS OF COLOR REACTIONS OF PHENOLS. (4). STUDIES ON REACTION OF RESORCINOL.]
• [Second metacarpal bone: RA(CXD, DIP), DXA]