Literature DB >> 12079877

A novel Mammalian homologue of a bacterial citrate-metabolizing enzyme.

Charlotte Söderberg1, Peter Lind.   

Abstract

Mammals metabolize citrate to acetyl-CoA and oxaloacetate via the enzyme, ATP:citrate lyase. Bacteria lack this enzyme, but have the ability to cleave citrate in the form of citryl-CoA in an analogous manner using a structurally distinct enzyme. We have identified a novel mammalian gene that shows significant amino acid sequence homology to the bacterial CitE gene product that is responsible for cleavage of citryl-CoA. We propose that this gene encodes an enzyme that catalyzes cleavage of substrates related to CoA esters of citrate or an analogous intermediary metabolite. The product of this novel gene may represent a component of an unknown metabolic pathway in mammals.

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Year:  2002        PMID: 12079877     DOI: 10.1111/j.1749-6632.2002.tb04305.x

Source DB:  PubMed          Journal:  Ann N Y Acad Sci        ISSN: 0077-8923            Impact factor:   5.691


  3 in total

1.  Proteomic analysis of streptomycin resistant and sensitive clinical isolates of Mycobacterium tuberculosis.

Authors:  Prashant Sharma; Bhavnesh Kumar; Yash Gupta; Neelja Singhal; Vishwa Mohan Katoch; Krishnamurthy Venkatesan; Deepa Bisht
Journal:  Proteome Sci       Date:  2010-11-18       Impact factor: 2.480

2.  An essential bifunctional enzyme in Mycobacterium tuberculosis for itaconate dissimilation and leucine catabolism.

Authors:  Hua Wang; Alexander A Fedorov; Elena V Fedorov; Debbie M Hunt; Angela Rodgers; Holly L Douglas; Acely Garza-Garcia; Jeffrey B Bonanno; Steven C Almo; Luiz Pedro Sório de Carvalho
Journal:  Proc Natl Acad Sci U S A       Date:  2019-07-18       Impact factor: 12.779

3.  Citrate lyase CitE in Mycobacterium tuberculosis contributes to mycobacterial survival under hypoxic conditions.

Authors:  Jialing Hu; Kaixi Jin; Zheng-Guo He; Hua Zhang
Journal:  PLoS One       Date:  2020-04-17       Impact factor: 3.240

  3 in total

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