Information on EC 1.1.1.77 - lactaldehyde reductase

Word Map on EC 1.1.1.77
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)


The expected taxonomic range for this enzyme is: Bacteria, Eukaryota

EC NUMBER
COMMENTARY hide
1.1.1.77
-
RECOMMENDED NAME
GeneOntology No.
lactaldehyde reductase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
(R)[or (S)]-propane-1,2-diol + NAD+ = (R)[or (S)]-lactaldehyde + NADH + H+
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
-
-
-
-
reduction
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
ethylene glycol degradation
-
-
L-lactaldehyde degradation (anaerobic)
-
-
methylglyoxal degradation VI
-
-
L-lactaldehyde degradation
-
-
Glyoxylate and dicarboxylate metabolism
-
-
Propanoate metabolism
-
-
Microbial metabolism in diverse environments
-
-
SYSTEMATIC NAME
IUBMB Comments
(R)[or (S)]-propane-1,2-diol:NAD+ oxidoreductase
-
CAS REGISTRY NUMBER
COMMENTARY hide
37250-15-0
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain VPI-5482, gene rhaO
-
-
Manually annotated by BRENDA team
strain VPI-5482, gene rhaO
-
-
Manually annotated by BRENDA team
Microcyclus eburneus
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(R)-propane-1,2-diol + NAD+
(R)-lactaldehyde + NADH
show the reaction diagram
(S)-propane-1,2-diol + NAD+
(S)-lactaldehyde + NADH
show the reaction diagram
ethanol + NAD+
acetaldehyde + NADH
show the reaction diagram
ethylene glycol + NAD+
glycolaldehyde + NAD+
show the reaction diagram
-
-
-
-
r
glycerol + NAD+
DL-glyceraldehyde + NADH
show the reaction diagram
-
-
-
-
r
L-1,2-propanediol + NAD+
L-lactaldehyde + NADH + H+
show the reaction diagram
propanol + NAD+
propionaldehyde + NADH
show the reaction diagram
-
-
-
-
r
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
(S)-propane-1,2-diol + NAD+
(S)-lactaldehyde + NADH
show the reaction diagram
L-1,2-propanediol + NAD+
L-lactaldehyde + NADH + H+
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADP+
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ascorbate
-
0.025 mM FeCl3 and 0.035 mM ascorbate causes a 90% enzyme inactivation after 120 min = inactivation of metal-catalyzed oxidation; several amino-acids prevent the inactivation; under aerobic conditions 0.025 mM FeCl3 causes a 50% enzyme inactivation after 120 min
Fe2+
-
under anaerobic conditions 0.01 mM Fe2+ and 0.1 mM H2O2 had the effect of 85% enzyme inactivation after 2 min, with addition of 0.0001 mM catalase the inactivation is only 25% after 2 min and with addition of 0.01 mM superoxide dismutase instead of catalse the inactivation is again 82% after 2 min
Fe3+
-
0.025 mM FeCl3 and 0.035 mM ascorbate causes a 90% enzyme inactivation after 120 min = inactivation of metal-catalyzed oxidation; several amino-acids prevent the inactivation; under aerobic conditions 0.025 mM FeCl3 causes a 50% enzyme inactivation after 120 min
H2O2
-
under anaerobic conditions 0.01 mM Fe2+ and 0.1 mM H2O2 had the effect of 85% enzyme inactivation after 2 min, with addition of 0.0001 mM catalase the inactivation is only 25% after 2 min and with addition of 0.01 mM superoxide dismutase instead of catalse the inactivation is again 82% after 2 min
iodoacetate
-
-
L-1,2-propanediol
-
above 25 mM: substrate inhibition
N-ethylmaleimide
-
-
p-chloromercuribenzoate
-
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.065
acetaldehyde
-
-
11
DL-1,2-Propanediol
-
-
0.56
DL-lactaldehyde
-
-
0.26
ethanol
-
-
1.25
L-1,2-propanediol
-
pH 9.5
0.035
L-lactaldehyde
-
pH 7.0
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
36.6
Microcyclus eburneus
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
9.5
-
dehydrogenation of L-1,2-propanediol
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.5 - 10
-
reduction of lactaldehyde, pH 4.5: 50% of reductase activity maximum, pH 10: 10% of reductase activity maximum
6 - 7.8
-
reduction of DL-lactaldehyde, pH 6: 50% of reductase activity maximum, pH 7.8: 45% of reductase activity maximum
8 - 11
-
dehydrogenation of 1,2-propanediol, pH 8: 10% of dehydrogenase activity maximum, pH 11: 65% of dehydrogenase activity maximum
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25
-
enzyme assay performed at this temperature
30
-
enzyme assay performed at this temperature
43
-
enzyme assay performed at this temperature
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25 - 43
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
PDB
SCOP
CATH
ORGANISM
UNIPROT
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
76000
-
gel permeation chromatography on a calibrated column of Ultrogel AcA 34 under denaturating conditions
155000
Microcyclus eburneus
-
gel filtration on Sephadex G-200
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
-
2 * 39000, SDS-PAGE
tetramer
Microcyclus eburneus
-
4 * 38000, SDS-PAGE
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
crude extract, ammonium sulfate precipitation, heat treatment, ultrogel AcA 34 fractionation, DEAE-Sephadex column chromatography, second ultrogel AcA 34 fractionation
-
crude extract, protamine sulfate, ammonium sulfate, DEAE-Sephadex-25, hydroxylapatite, blue dextran polyacrylamide
Microcyclus eburneus
-
extraction, heat treatment, ammonium sulfate-fractionation, DEAE-cellulose and Alumina C
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
gene rhaO, encoded in the rhaKIPAO gene cluster, expression analysis, transcriptional regulation of the rhaKIPAOR gene cluster, overview
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
synthesis
-
fermentation of L-rhamnose, L-fucose and D-fucose to a mixture of 1,2-propanediol, acetone, H2, CO2 and ethanol
Show AA Sequence (526 entries)
Please use the Sequence Search for a certain query.