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Literature summary extracted from

  • Crow, V.L.
    Properties of 2,3-butanediol dehydrogenase from Lactococcus lactis subsp. lactis in relation to citrate fermentation (1990), Appl. Environ. Microbiol., 56, 1656-1665.
    View publication on PubMedView publication on EuropePMC

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.1.1.4 170000
-
 enzyme 1 and 2, gel filtration Lactococcus lactis

Organism

EC Number Organism UniProt Comment Textmining
1.1.1.4 Lactococcus lactis
-
 2,3-butanediol dehydrogenase 1 and 2
-
1.1.1.4 Lactococcus lactis
-
 subsp. lactis D10
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.1.1.4 2,3-butanediol dehydrogenase 1 and 2 Lactococcus lactis
1.1.1.4 partially Lactococcus lactis

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.1.1.4 5.1
-
 acetoin, enzyme 1 Lactococcus lactis
1.1.1.4 7.55
-
 acetoin, enzyme 2 Lactococcus lactis
1.1.1.4 35.55
-
 diacetyl, enzyme 2 Lactococcus lactis
1.1.1.4 35.6
-
 diacetyl, enzyme 1 Lactococcus lactis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.1.4 2,3-butanediol + NAD+
-
 Lactococcus lactis acetoin + NADH
-
 r
1.1.1.4 acetoin + NADH + H+
-
 Lactococcus lactis 2,3-butanediol + NAD+ enzyme 1, only meso-2,3-butanediol is formed, enzyme 2 gives mixture of meso- and optical isomers r
1.1.1.4 diacetyl + NADH
-
 Lactococcus lactis 2,3-butanediol + NAD+ enzyme 1, only meso-2,3-butanediol is formed, enzyme 2 gives mixture of meso- and optical isomers r

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.1.1.4 5.8
-
 substrate reduction, enzyme 1 Lactococcus lactis
1.1.1.4 6.1
-
 substrate reduction, enzyme 2 Lactococcus lactis
1.1.1.4 8.5
-
 substrate oxidation, enzyme 2 Lactococcus lactis
1.1.1.4 10
-
 substrate oxidation, enzyme 1 Lactococcus lactis