A structural phylogeny for understanding 2-oxoacid oxidoreductase function.

Abstract:

:2-Oxoacid:ferredoxin oxidoreductases (OFORs) are essential enzymes in microbial one-carbon metabolism. They use thiamine pyrophosphate to reversibly cleave carbon-carbon bonds, generating low potential (∼-500mV) electrons. Crystallographic analysis of a recently discovered OFOR, an oxalate oxidoreductase (OOR), has provided a second view of OFOR architecture and active site composition. Using these recent structural data along with the previously determined structures of pyruvate:ferredoxin oxidoreductase, structure-function relationships in this superfamily have been expanded and re-evaluated. Additionally, structural motifs have been defined that better serve to distinguish one OFOR subfamily from another and potentially uncover novel OFORs.

journal_name

Curr Opin Struct Biol

authors

Gibson MI,Chen PY,Drennan CL

doi

10.1016/j.sbi.2016.05.011

subject

Has Abstract

pub_date

2016-12-01 00:00:00

pages

54-61

eissn

0959-440X

issn

1879-033X

pii

S0959-440X(16)30046-X

journal_volume

41

pub_type

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