Literature DB >> 17146529

Mechanism and substrate stereochemistry of 2-amino-3-oxobutyrate CoA ligase: implications for 5-aminolevulinate synthase and related enzymes.

Qamar Bashir1, Naeem Rashid, Muhammad Akhtar.   

Abstract

The condensation process catalysed by 2-amino-3-oxobutyrate CoA ligase (KBL; also known as 2-amino-3-ketobutyrate ligase) involves the loss of the pro-R hydrogen atom of glycine and occurs with the inversion of stereochemistry; a similar scenario is envisaged for the condensation step of other alpha-oxoamine synthases.

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Year:  2006        PMID: 17146529     DOI: 10.1039/b609925d

Source DB:  PubMed          Journal:  Chem Commun (Camb)        ISSN: 1359-7345            Impact factor:   6.222


  1 in total

1.  Use of isotopically labeled substrates reveals kinetic differences between human and bacterial serine palmitoyltransferase.

Authors:  Peter J Harrison; Kenneth Gable; Niranjanakumari Somashekarappa; Van Kelly; David J Clarke; James H Naismith; Teresa M Dunn; Dominic J Campopiano
Journal:  J Lipid Res       Date:  2019-02-21       Impact factor: 5.922

  1 in total

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