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Enzyme Nomenclature
Information on EC 1.1.1.77 - lactaldehyde reductase
for references in articles please use BRENDA:EC1.1.1.77
Word Map on EC 1.1.1.77
- 1.1.1.77
- l-fucose
- l-1,2-propanediol
- l-rhamnose
-
nad-linked
-
dissimilation
-
aldolase
-
klebsiella
- typhimurium
- l-lactate
- dihydroxyacetone
-
1-phosphate
- subtilisin
- pneumoniae
-
dinucleotide-linked
-
metal-catalyzed
-
bacteriol
- zymomonas
- mobilis
-
iron-containing
-
permease
-
metal-binding
-
noninducible
-
fuculose
-
laczya
-
rhamnose-induced
-
anaerobiosis
-
six-carbon
-
rha
-
irretrievably
- synthesis
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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
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EC NUMBER 
COMMENTARY 
1.1.1.77
-
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RECOMMENDED NAME
GeneOntology No.
lactaldehyde reductase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
(R)[or (S)]-propane-1,2-diol + NAD+ = (R)[or (S)]-lactaldehyde + NADH + H+
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
reduction
-
-
-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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SYSTEMATIC NAME
IUBMB Comments
(R)[or (S)]-propane-1,2-diol:NAD+ oxidoreductase
-
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CAS REGISTRY NUMBER
COMMENTARY
37250-15-0
-
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(R)-propane-1,2-diol + NAD+
(R)-lactaldehyde + NADH
-
-
-
-
?
(R)-propane-1,2-diol + NAD+
(R)-lactaldehyde + NADH
-
acts only on L-isomer
-
-
?
(R)-propane-1,2-diol + NAD+
(R)-lactaldehyde + NADH
-
utilizes D- and L-lactaldehyde in the reverse direction equally well
-
-
r
(S)-propane-1,2-diol + NAD+
(S)-lactaldehyde + NADH
-
in the fermentative metabolism 1,2-propanediol is formed under phosphate limitation via the methylglyoxal by-pass
-
-
-
(S)-propane-1,2-diol + NAD+
(S)-lactaldehyde + NADH
-
only L-propane-1,2-diol is oxidized
-
-
-
(S)-propane-1,2-diol + NAD+
(S)-lactaldehyde + NADH
-
anaerobically lactaldehyde is reduced to propane-1,2-diol in the L-fucose and L-rhamnose metabolism
-
-
-
(S)-propane-1,2-diol + NAD+
(S)-lactaldehyde + NADH
-
aerobically only mutant, strain 3 and 430, are capable of growth on 1,2-propanediol
-
-
-
(S)-propane-1,2-diol + NAD+
(S)-lactaldehyde + NADH
-
Embden-Meyerhof pathway for 6-deoxyhexose catabolism
-
-
?
L-1,2-propanediol + NAD+
L-lactaldehyde + NADH + H+
-
-
-
-
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(S)-propane-1,2-diol + NAD+
(S)-lactaldehyde + NADH
-
in the fermentative metabolism 1,2-propanediol is formed under phosphate limitation via the methylglyoxal by-pass
-
-
-
(S)-propane-1,2-diol + NAD+
(S)-lactaldehyde + NADH
-
anaerobically lactaldehyde is reduced to propane-1,2-diol in the L-fucose and L-rhamnose metabolism
-
-
-
(S)-propane-1,2-diol + NAD+
(S)-lactaldehyde + NADH
-
aerobically only mutant, strain 3 and 430, are capable of growth on 1,2-propanediol
-
-
-
(S)-propane-1,2-diol + NAD+
(S)-lactaldehyde + NADH
-
Embden-Meyerhof pathway for 6-deoxyhexose catabolism
-
-
?
L-1,2-propanediol + NAD+
L-lactaldehyde + NADH + H+
-
-
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NADP+
-
cell extracts also contain lactaldehyde reductase activity which utilizes either NADH or NADPH as electron donor
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
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
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
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
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25 - 43
25 - 43
-
optimal temperature for enzyme activity differs in various organisms
25 - 43
-
optimal temperature for enzyme activity differs in various organisms
25 - 43
-
optimal temperature for enzyme activity differs in various organisms
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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PDB
SCOP
CATH
UNIPROT
ORGANISM
Escherichia coli (strain K12);
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
76000
-
gel permeation chromatography on a calibrated column of Ultrogel AcA 34 under denaturating conditions
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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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
-
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
gene rhaO, encoded in the rhaKIPAO gene cluster, expression analysis, transcriptional regulation of the rhaKIPAOR gene cluster, overview
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
a rhaO knockout mutant produces reduced levels of L-1,2-propanediol during growth in rhamnose, the mutant cannot utilise rhamnose as the sole carbon source but grows normally on glucose
additional information
-
a rhaO knockout mutant produces reduced levels of L-1,2-propanediol during growth in rhamnose, the mutant cannot utilise rhamnose as the sole carbon source but grows normally on glucose
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
-
fermentation of L-rhamnose, L-fucose and D-fucose to a mixture of 1,2-propanediol, acetone, H2, CO2 and ethanol
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LINKS TO OTHER DATABASES (specific for EC-Number 1.1.1.77)
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