Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary 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

Application

EC Number Application Comment Organism
1.1.99.30 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

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

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.1.99.30 Molybdenum required Proteus vulgaris

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.1.99.30 64000
-
 x * 80000 + x * 64000, alpha,beta-structure Proteus vulgaris
1.1.99.30 80000
-
 x * 80000 + x * 64000, alpha,beta-structure Proteus vulgaris
1.1.99.30 600000
-
 above Proteus vulgaris

Organism

EC Number Organism UniProt Comment Textmining
1.1.99.30 Proteus vulgaris
-
-
-

Reaction

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

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.1.99.30 1000
-
 purified enzyme Proteus vulgaris

Storage Stability

EC Number Storage Stability Organism
1.1.99.30 -15°C, loss of 10% activity within 1-2 years Proteus vulgaris
1.1.99.30 room temperature, freeze dried cells, loss of 10% of activity within 1-2 years Proteus vulgaris

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.99.30 (2S,3R,4S)-2-hydroxy-3-halogenbutyrolactones + reduced benzyl viologen highly stereospecific reaction Proteus vulgaris ?
-
 r
1.1.99.30 (2S,3R,4S)-2-hydroxy-3-halogenbutyrolactones + reduced methyl viologen highly stereospecific reaction Proteus vulgaris ?
-
 r
1.1.99.30 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
1.1.99.30 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
1.1.99.30 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

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

Synonyms

EC Number Synonyms Comment Organism
1.1.99.30 (2R)-hydroxycarboxlate-viologen-oxidoreductase
-
 Proteus vulgaris
1.1.99.30 2-oxoacid reductase
-
 Proteus vulgaris
1.1.99.30 D-2-hydroxy acid dehydrogenase
-
 Proteus vulgaris
1.1.99.30 dehydrogenase, D-2-hydroxy acid
-
 Proteus vulgaris
1.1.99.30 HVOR
-
 Proteus vulgaris
1.1.99.30 hydroxycarboxlate-viologen-oxidoreductase
-
 Proteus vulgaris

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.1.99.30 8.5
-
-
 Proteus vulgaris

Cofactor

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