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Literature summary for 1.1.99.30 extracted from

  • Simon, H.
    Properties and mechanistic aspects of newly found redox enzymes from anaerobes suitable for bioconversions on preparatory scale (1993), Indian J. Chem. B, 32, 170-175.
No PubMed abstract available
Search for more literature for 1.1.99.30

Application

Application Comment Organism
synthesis enzyme can be used as a stereospecific biocatalyst for production of a wide range of compounds, e.g. 3-enoic-, 3,5-dienoic-, and 4-oxo-3R,S-hydroxyacids Proteus vulgaris

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane bound Proteus vulgaris 16020
-

Metals/Ions

Metals/Ions Comment Organism Structure
Molybdenum required Proteus vulgaris

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
64000
-
 x * 80000 + x * 64000, alpha,beta-structure Proteus vulgaris
80000
-
 x * 80000 + x * 64000, alpha,beta-structure Proteus vulgaris
600000
-
 above Proteus vulgaris

Organism

Organism UniProt Comment Textmining
Proteus vulgaris
-
-
-

Reaction

Reaction Comment Organism Reaction ID
a (2R)-hydroxy-carboxylate + acceptor = a 2-oxo-carboxylate + reduced acceptor mechanism Proteus vulgaris
a

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1000
-
 purified enzyme Proteus vulgaris

Storage Stability

Storage Stability Organism
-15°C, loss of 10% activity within 1-2 years Proteus vulgaris
room temperature, freeze dried cells, loss of 10% of activity within 1-2 years Proteus vulgaris

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(2S,3R,4S)-2-hydroxy-3-halogenbutyrolactones + reduced benzyl viologen highly stereospecific reaction Proteus vulgaris ?
-
 r
(2S,3R,4S)-2-hydroxy-3-halogenbutyrolactones + reduced methyl viologen highly stereospecific reaction Proteus vulgaris ?
-
 r
2-oxo-carboxylate + reduced benzyl viologen stereospecific, very wide substrate specificity, reduces 2-oxo-carboxylates with diverse types of residues at position 3, such as unbranched and branched alkyl, hydroxy, one or two conjugated carbon carbon double bonds, additional CO, and -OOC(CH2)n, overview Proteus vulgaris (2R)-hydroxy-carboxylate + oxidized benzyl viologen
-
 r
2-oxo-carboxylate + reduced methyl viologen stereospecific, very wide substrate specificity, reduces 2-oxo-carboxylates with diverse types of residues at position 3, such as unbranched and branched alkyl, hydroxy, one or two conjugated carbon carbon double bonds, additional CO, and -OOC(CH2)n, overview Proteus vulgaris (2R)-hydroxy-carboxylate + oxidized methyl viologen
-
 r
additional information 2-oxo acids with diverse substituents, e.g. carboxy, methyl, ethyl, halogen, methoxy, thiomethyl, NHCHO, unbranched and branched alkyl, OH-containing residues in 3-position, double bonds containing residues, substituents with additional CO groups, -OOC(CH2)n with n being at least 3, overview Proteus vulgaris ?
-
 ?

Subunits

Subunits Comment Organism
oligomer x * 80000 + x * 64000, alpha,beta-structure Proteus vulgaris

Synonyms

Synonyms Comment Organism
(2R)-hydroxycarboxlate-viologen-oxidoreductase
-
 Proteus vulgaris
2-oxoacid reductase
-
 Proteus vulgaris
D-2-hydroxy acid dehydrogenase
-
 Proteus vulgaris
dehydrogenase, D-2-hydroxy acid
-
 Proteus vulgaris
HVOR
-
 Proteus vulgaris
hydroxycarboxlate-viologen-oxidoreductase
-
 Proteus vulgaris

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8.5
-
-
 Proteus vulgaris

Cofactor

Cofactor Comment Organism Structure
molybdenum cofactor i.e. MoCo Proteus vulgaris
additional information neither NADH nor NADPH are cosubstrates for the enzyme, no flavin or heme cofactors Proteus vulgaris