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Delineating the reaction mechanism of reductase domains of Nonribosomal Peptide Synthetases from mycobacteria.

Abstract：

:Substrate binding to enzymes often follows a precise order where catalysis is accomplished through programmed conformational changes. Short-chain dehydrogenase/reductase (SDR) enzymes follow sequential order 'bi-bi' reaction kinetics. The mechanistic study of a SDR homolog, reductase (R) domain, from multifunctional enzymes, e.g. Nonribosomal Peptide Synthetases (NRPSs) and Polyketide Synthases (PKSs) has revealed that it reductively releases 4'-phosphopantetheinyl arm-tethered peptidyl product. We report that the R-domains of NRPSs from Mycobacterium tuberculosis (RNRP) and Mycobacterium smegmatis (RGPL) do not strictly adhere to the obligatory mode of catalysis performed by SDRs, but instead can carry out reductive catalysis of substrate following random bi-bi reaction mechanism as deciphered by NMR and SAXS studies. The crucial conformational change associated with NADPH binding necessary to achieve catalytically competent conformation is also delineated by SAXS studies. Using ITC, we have demonstrated that mutation of catalytic tyrosine to phenylalanine in R-domains results in 3-4-fold decrease in affinity for NADPH and attribute this phenomenon to loss of the noncovalent cation-π interactions present between the tyrosine and nicotinamide ring. We propose that the adaptation to an alternative theme of bi-bi catalytic mechanism enables the R-domains to process the substrates transferred by upstream domains and maintain assembly-line enzymology.

journal_name

J Struct Biol

journal_title

Journal of structural biology

authors

Haque AS,Patel KD,Deshmukh MV,Chhabra A,Gokhale RS,Sankaranarayanan R

doi

10.1016/j.jsb.2014.07.008

subject

Has Abstract

pub_date

2014-09-01 00:00:00

pages

207-214

issue

3

eissn

1047-8477

issn

1095-8657

pii

S1047-8477(14)00166-X

journal_volume

187

pub_type

杂志文章

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