1.8.1.5: 2-oxopropyl-CoM reductase (carboxylating)

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For detailed information about 2-oxopropyl-CoM reductase (carboxylating), go to the full flat file.

Reaction

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)

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Results	in table
6	AA Sequence
1	CAS Registry Number
3	Cloned(Commentary)
13	Cofactor
4	Crystallization (Commentary)
2	General Information
4	Inhibitors
2	kcat/KM [mM/s]
3	KM Value [mM]
2	Molecular Weight [Da]
9	Natural Substrates/ Products (Substrates)
31	Organism
2	Pathway
16	PDB ID
1	pH Optimum
9	Protein Variants
2	Purification (Commentary)
3	Reaction
3	Reaction Type
13	Reference
2	Specific Activity [micromol/min/mg]
28	Substrates and Products (Substrate)
5	Subunits
16	Synonyms
1	Systematic Name
1	Temperature Optimum [°C]
3	Turnover Number [1/s]

Crystallization

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

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CRYSTALLIZATION (Commentary)

ORGANISM

UNIPROT

LITERATURE

enzyme free or bound to substrate 2-ketopropyl-CoM, X-ray structure determination and analysis at 1.6-3.5 A resolution, multiple isomorphous replacement and anomalous scattering using four weak heavy atom derivatives

Xanthobacter autotrophicus

Q56839

657919

hanging drop vapour diffusion method

Xanthobacter autotrophicus

Q56839

672063

in complex with acetoacetate and 2-mercaptoethanesulfonate. In the substrate encapsulated state of the enzyme, CO2 is bound at the base of a narrow hydrophobic substrate access channel. The base of the channel is demarcated by a transition from a hydrophobic to hydrophilic environment where CO2 is located in position for attack on the carbanion of the ketopropyl group of the substrate to ultimately produce acetoacetate. This binding mode effectively discriminates against H2O and prevents protonation of the ketopropyl leaving group

Xanthobacter autotrophicus

Q56839

725008

vapor diffusion method, using 0.17 M ammonium acetate, 0.085 M trisodium citrate, pH 5.6, 27% (w/v) PEG 4000, and 15% (v/v) glycerol

Xanthobacter autotrophicus

Q56839

765078