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1.8.1.5: 2-oxopropyl-CoM reductase (carboxylating)

This is an abbreviated version!
For detailed information about 2-oxopropyl-CoM reductase (carboxylating), go to the full flat file.

Word Map on EC 1.8.1.5

Reaction

2-mercaptoethanesulfonate
+
acetoacetate
 +
NADP+
=
2-(2-oxopropylthio)ethanesulfonate
 +
CO2
 +
NADPH
 +
H+

Synonyms

2-ketopropyl coenzyme M oxidoreductase/carboxylase, 2-ketopropyl-coenzyme M oxidoreductase/carboxylase, 2-KPCC, More, NADPH:2-(2-ketopropylthio)ethanesulfonate oxidoreductase/carboxylase, NADPH:2-ketopropyl-coenzyme M carboxylase/oxidoreductase, NADPH:2-ketopropyl-coenzyme M oxidoreductase/carboxylase, NADPH:2-ketopropyl-CoM oxidoreductase/carboxylase, xecC

ECTree

     1 Oxidoreductases
         1.8 Acting on a sulfur group of donors
             1.8.1 With NAD+ or NADP+ as acceptor
                1.8.1.5 2-oxopropyl-CoM reductase (carboxylating)

Engineering

Engineering on EC 1.8.1.5 - 2-oxopropyl-CoM reductase (carboxylating)

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C82A
mutagenesis of the interchange thiol, abolishes all redox-dependent reactions. Redox-independent acetoacetate decarboxylation is not decreased
C87A
mutagenesis of the flavin thiol, results in an inactive enzyme for steady-state redox-dependent reactions, but this variant catalyzes a single-turnover reaction producing a 0.8:1 ratio of product to enzyme. Redox-independent acetoacetate decarboxylation is not decreased
F501H
the mutant shows 10% acetoacetate production activity compared to the wild type enzyme. The overall rate of NADPH turnover remains relatively unchanged in the F501H variant relative to wild type. Moreover, acetone formation by F501H is comparable in rate to the carboxylation reaction catalyzed by wild type enzyme and leading to acetoacetate
F501H/H506E
H137A
mutagenesis of the histidine proximal to the ordered water molecule, leads to nearly complete loss of redox-dependent reactions. Redox-independent acetoacetate decarboxylation is not decreased
H506E
the mutant shows 37% acetoacetate production activity compared to the wild type enzyme. NADPH turnover is around 1.5fold slower in H506E versus wild type enzyme
H84A
mutagenesis of the distal histidine residue, reduces the redox-dependent activities by 58 to 76%. Redox-independent acetoacetate decarboxylation is not decreased
M140A
residue flanking the substrate, catalytic efficiency for 2-(2-oxopropylthio)ethanesulfonate carboxylation is 47fold lower than that for wild-type