Literature DB >> 6628689

A mechanism for the transfer of the carboxyl-group from 1'-N-carboxybiotin to acceptor substrates by biotin-containing enzymes.

G J Goodall, R Prager, J C Wallace, D B Keech.   

Abstract

Previous proposals for the mechanism by which biotin-dependent enzymes catalyse the transfer of the carboxyl group from 1'-N-carboxybiotin to acceptor molecules do not appear to be consistent with all of the experimental observations now available. We propose a multi-step mechanism in which (a) substrate and then carboxybiotin bind at the second partial reaction site, (b) a base positioned adjacent to the 3'-N of the carboxybiotin abstracts a proton from the 3'-N and (c) the resulting enolate ion and the acceptor substrate undergo a concerted reaction resulting in carboxyl-group transfer.

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Year:  1983        PMID: 6628689     DOI: 10.1016/0014-5793(83)81150-8

Source DB:  PubMed          Journal:  FEBS Lett        ISSN: 0014-5793            Impact factor:   4.124


  1 in total

1.  Oxamate is an alternative substrate for pyruvate carboxylase from Rhizobium etli.

Authors:  John F Marlier; W W Cleland; Tonya N Zeczycki
Journal:  Biochemistry       Date:  2013-04-18       Impact factor: 3.321

  1 in total

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