Home LiteratureArticle Details

PMID: 1743516 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

A bacterial homolog to the mitochondrial enoyl-CoA hydratase.

Gene ·Vol. 107 ·No. 1 ·1991-10-30 ·Pages 171-2

Beckman DL, Kranz RG

Abstract

A 257-amino acid (aa) open reading frame in the photosynthetic bacterium, Rhodobacter capsulatus, shows significant homology to the mitochondrial enoyl-CoA hydratase (290 aa). This similarity in size and sequence suggests that R. capsulatus oxidizes fatty acids using specific components, more like the mitochondrial system than the multifunctional component system of Escherichia coli.

MeSH Terms

Amino Acid Sequence Animals Base Sequence Enoyl-CoA Hydratase/genetics Mitochondria/enzymology Molecular Sequence Data Open Reading Frames/genetics Rats Rhodobacter capsulatus/enzymology,genetics Sequence Homology, Nucleic Acid

Chemicals

Enoyl-CoA Hydratase

Authors & Affiliations

2 authors, click to expand affiliations / ORCID

Beckman D L

Department of Biology, Washington University, St. Louis, MO 63130.

Kranz R G

Article Info

Journal

Gene

Abbr.

Gene

ISSN

0378-1119

DOI

10.1016/0378-1119(91)90313-z

Published

1991-10-30

Pages

171-2

Language

English

Region

Netherlands

NLM ID

7706761

Subset

Grants

NCRR NIH HHS · BRSGS07 RR077054 · United States

NIGMS NIH HHS · GM 39106 · United States

Databases

GENBANK

M59727, M59728, S68775, S69445, S69486, S69499, S69505, S69519, S69521, X60194

External Links

PubMed source DOI: 10.1016/0378-1119(91)90313-z View journal details

Analysis Services

A bacterial homolog to the mitochondrial enoyl-CoA hydratase.

Contact

WeChat Official Account