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Information on EC 1.1.1.60 - 2-hydroxy-3-oxopropionate reductase
for references in articles please use BRENDA:EC1.1.1.60
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EC Tree 1 Oxidoreductases
1.1 Acting on the CH-OH group of donors
1.1.1 With NAD+ or NADP+ as acceptor
1.1.1.60 2-hydroxy-3-oxopropionate reductase
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
- 1.1.1.60
-
beta-hydroxyacids
- dehydrogenases
- nad+
- d-threonine
- hydroxypyruvate
-
nadp+-dependent
-
carboligase
- aldolase
- glyoxylate
- influenzae
- galactarate
- dehydratase
showSynonyms
tartronate semialdehyde reductase, beta-hydroxyacid dehydrogenase, 2-hydroxy-3-oxopropionate reductase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
beta-hydroxyacid dehydrogenase
tartronate semialdehyde reductase
TSAR
additional information
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the enzyme belongs to family of structurally and mechanically related beta-hydroxyacid dehydrogenases, COG2084
tartronate semialdehyde reductase
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tartronate semialdehyde reductase
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tartronate semialdehyde reductase
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TSAR
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
D-glycerate + NAD(P)+ = 2-hydroxy-3-oxopropanoate + NAD(P)H + H+
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
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redox reaction
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reduction
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-
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PATHWAY SOURCE
PATHWAYS
BRENDA
MetaCyc
D-galactarate degradation I, D-glucarate degradation I, glycolate and glyoxylate degradation I
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SYSTEMATIC NAME
IUBMB Comments
D-glycerate:NAD(P)+ oxidoreductase
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CAS REGISTRY NUMBER
COMMENTARY
9028-68-6
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2-hydroxy-3-oxopropanoate + NADH + H+
D-glycerate + NAD+
Substrates: -
Products: -
Products: -
?
D-glycerate + NADP+
2-hydroxy-3-oxopropanoate + NADPH + H+
Substrates: enzyme shows strong specificity and enantioselectivity for D-glycerate
Products: -
Products: -
?
hydroxypyruvate + NAD(P)H + H+
glycerate + NAD(P)+
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Substrates: -
Products: -
Products: -
r
L-glycerate + NADP+
2-hydroxy-3-oxopropanoate + NADPH + H+
Substrates: enzyme shows strong specificity and enantioselectivity for D-glycerate
Products: -
Products: -
?
malonic semialdehyde + NADH
3-hydroxypropanoate + NAD+
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Substrates: -
Products: -
Products: -
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mesoxalic semialdehyde + NADH
hydroxypyruvate + NAD+
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Substrates: -
Products: -
Products: -
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tartronate semialdehyde + NADH
(R)-glycerate + NAD+
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Substrates: as cofactor in the final stage of D-glycerate biosynthesis
Products: -
Products: -
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tartronate semialdehyde + NADH + H+
(R)-glycerate + NAD+
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Substrates: -
Products: -
Products: -
?
(R)-glycerate + NAD(P)+
tartronate semialdehyde + NAD(P)H
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Substrates: -
Products: -
Products: -
?
(R)-glycerate + NAD(P)+
tartronate semialdehyde + NAD(P)H
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Substrates: -
Products: -
Products: -
r
(R)-glycerate + NAD(P)+
tartronate semialdehyde + NAD(P)H
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Substrates: -
Products: -
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?
(R)-glycerate + NAD(P)+
tartronate semialdehyde + NAD(P)H
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Substrates: -
Products: -
Products: -
r
(R)-glycerate + NAD(P)+
tartronate semialdehyde + NAD(P)H
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Substrates: -
Products: -
Products: -
r
tartronate semialdehyde + NAD(P)H
(R)-glycerate + NAD(P)+
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Substrates: -
Products: -
Products: -
?
tartronate semialdehyde + NAD(P)H
(R)-glycerate + NAD(P)+
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Substrates: -
Products: -
Products: -
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tartronate semialdehyde + NAD(P)H
(R)-glycerate + NAD(P)+
-
Substrates: -
Products: -
Products: -
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tartronate semialdehyde + NAD(P)H
(R)-glycerate + NAD(P)+
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Substrates: -
Products: -
Products: -
r
tartronate semialdehyde + NAD(P)H
(R)-glycerate + NAD(P)+
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Substrates: -
Products: -
Products: -
?
tartronate semialdehyde + NAD(P)H
(R)-glycerate + NAD(P)+
-
Substrates: -
Products: -
Products: -
r
tartronate semialdehyde + NAD(P)H
(R)-glycerate + NAD(P)+
-
Substrates: -
Products: -
Products: -
r
tartronate semialdehyde + NAD(P)H
(R)-glycerate + NAD(P)+
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Substrates: NADH 3 times more effective than NADPH
Products: -
Products: -
r
tartronate semialdehyde + NAD(P)H
(R)-glycerate + NAD(P)+
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Substrates: -
Products: -
Products: -
?
additional information
?
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Substrates: poor activity towards 6-phosphogluconic acid, beta-hydroxybutyric acid and D-threonine
Products: -
Products: -
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additional information
?
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Substrates: poor activity towards 6-phosphogluconic acid, beta-hydroxybutyric acid and D-threonine
Products: -
Products: -
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
tartronate semialdehyde + NADH
(R)-glycerate + NAD+
-
Substrates: as cofactor in the final stage of D-glycerate biosynthesis
Products: -
Products: -
?
tartronate semialdehyde + NAD(P)H
(R)-glycerate + NAD(P)+
-
Substrates: -
Products: -
Products: -
?
tartronate semialdehyde + NAD(P)H
(R)-glycerate + NAD(P)+
-
Substrates: -
Products: -
Products: -
?
tartronate semialdehyde + NAD(P)H
(R)-glycerate + NAD(P)+
-
Substrates: -
Products: -
Products: -
r
tartronate semialdehyde + NAD(P)H
(R)-glycerate + NAD(P)+
-
Substrates: -
Products: -
Products: -
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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TURNOVER NUMBER [1/s]
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
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
over-expression of the gene results in improved glycerol assimilation. Glycolipid accumulation is reduced by 45.2% in the knockout mutant whereas over-expression of the gene increases it by 40.4%
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
26000
-
4 * 26000, sedimentation velocity after treatment with guanidine hydrochloride and mercaptoethanol, amino acid analysis
40000
2 * 40000, SDS-PAGE, 2 * 41000, calculated, recombinant protein
41000
2 * 40000, SDS-PAGE, 2 * 41000, calculated, recombinant protein
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
2 * 40000, SDS-PAGE, 2 * 41000, calculated, recombinant protein
tetramer
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4 * 26000, sedimentation velocity after treatment with guanidine hydrochloride and mercaptoethanol, amino acid analysis
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
enzyme with L-tartrate bound to the active site, sitting drop vapour diffusion method, mixing of 0.0005 ml of the protein solution, containing 107 mg/ml protein in in 10 mM HEPES pH 8.0, 200 mM NaCl, with 0.0005 ml of 0.1 M imidazole buffer pH 8.0, 1 M potassium/sodium L-tartrate and 0.2 M sodium chloride, and equilibrated at 16°C over 0.135 ml of this solution, overnight, X-ray diffraction structure determination and analysis at 1.65 A resolution, the single-wavelength anomalous diffraction method
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
2°C, suspension in ammonium sulfate, pH 7.5, 10% loss in 1 month
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4°C, Tris-HCl, pH 8.0, highly unstable, precipitates during storage
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
of recombinant protein
recombinant His6-tagged GarR from Escherichia coli strain BL21, the tag is removed by TEV protease, purification by nickel affinity chromatography
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene garR, expression of the His6-tagged enzyme in Escherichia coli strain BL21
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overexpression in Escherichia coli
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Dijkhuizen, L.; Knight, M.; Harder, W.
Metabolic regulation in Pseudomonas oxalaticus OX1. Autotrophic and heterotrophic growth on mixed substrates
Arch. Microbiol.
116
77-83
1978
Cupriavidus oxalaticus, Cupriavidus oxalaticus OX1
brenda
Van der Drift, C.; de Windt, F.E.
Glyoxylate conversion by Hyphomicrobium species grown on allantoin as nitrogen source
Antonie van Leeuwenhoek
49
167-172
1983
Hyphomicrobium sp.
brenda
Kohn, L.
Tartaric acid metabolism. 8. Crystalline tartronic semialdehyde reductase
J. Biol. Chem.
243
4426-4433
1968
Pseudomonas putida
brenda
Kornberg, H.L.; Gotto, A.M.
Tartronic semialdehyde reductase (crystalline)
Methods Enzymol.
9
240-247
1966
Pseudomonas putida
-
brenda
Gotto, A.M.; Kornberg, H.L.
The metabolism of C2 compounds in micro-organisms
Biochem. J.
81
273-284
1961
Pseudomonas putida
brenda
Ijau, R.K.; Herndon, C.A.; Hawes, J.W.
Novel beta-hydroxyacid dehydrogenases in Escherichia coli and Haemophilus infuenzae
J. Biol. Chem.
275
38780-38786
2000
Escherichia coli, Haemophilus influenzae
brenda
Njau, R.K.; Herndon, C.A.; Hawes, J.W.
New developments in our understanding of the beta-hydroxyacid dehydrogenases
Chem. Biol. Interact.
130-132
785-791
2001
Escherichia coli, Haemophilus influenzae
brenda
Osipiuk, J.; Zhou, M.; Moy, S.; Collart, F.; Joachimiak, A.
X-ray crystal structure of GarR - tartronate semialdehyde reductase from Salmonella typhimurium
J. Struct. Funct. Genomics
10
249-253
2009
Salmonella enterica subsp. enterica serovar Typhimurium
brenda
Liu, Y.; Koh, C.; Sun, L.; Ji, L.
Tartronate semialdehyde reductase defines a novel rate-limiting step in assimilation and bioconversion of glycerol in Ustilago maydis
PLoS ONE
6
e16438
2011
Ustilago maydis (A0A0D1DYW4), Ustilago maydis
brenda
Hoover, G.J.; Jorgensen, R.; Rochon, A.; Bajwa, V.S.; Merrill, A.R.; Shelp, B.J.
Identification of catalytically important amino acid residues for enzymatic reduction of glyoxylate in plants
Biochim. Biophys. Acta
1834
2663-2671
2013
Salmonella enterica subsp. enterica serovar Typhimurium (Q8ZLV8)
brenda
EXTERNAL LINKS (specific for EC-Number 1.1.1.60)
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