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EC Tree
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
decarboxylase, tartrate, More,
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decarboxylase, tartrate
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additional information
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enzyme resembles L-tartrate dehydrogenase/D-malate dehydrogenase from Rhodopseudomonas sphaeroides and tartrate dehydrogenase from Pseudomonas putida
additional information
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enzyme resembles L-tartrate dehydrogenase/D-malate dehydrogenase from Rhodopseudomonas sphaeroides and tartrate dehydrogenase from Pseudomonas putida
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(R,R)-tartrate = D-glycerate + CO2
(R,R)-tartrate = D-glycerate + CO2
reduction proceeds concomitantly with decarboxylation, but at a much lower rate
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(R,R)-tartrate = D-glycerate + CO2
reduction proceeds concomitantly with decarboxylation, but at a much lower rate
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(R,R)-tartrate = D-glycerate + CO2
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(R,R)-tartrate carboxy-lyase (D-glycerate-forming)
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D-malate + NAD+
pyruvate + CO2 + NADH
L-tartrate
D-glycerate + CO2
meso-tartrate
D-glycerate + CO2
oxaloacetate + NAD+
?
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?
additional information
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D-malate + NAD+
pyruvate + CO2 + NADH
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?
D-malate + NAD+
pyruvate + CO2 + NADH
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?
L-tartrate
D-glycerate + CO2
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?
L-tartrate
D-glycerate + CO2
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best substrate
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?
L-tartrate
D-glycerate + CO2
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best substrate
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?
L-tartrate
D-glycerate + CO2
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direct conversion, with almost 100% selectivity
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?
L-tartrate
D-glycerate + CO2
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inducible by L-tartrate
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?
L-tartrate
D-glycerate + CO2
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best substrate
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?
L-tartrate
D-glycerate + CO2
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direct conversion, with almost 100% selectivity
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?
L-tartrate
D-glycerate + CO2
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inducible by L-tartrate
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?
L-tartrate
D-glycerate + CO2
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?
L-tartrate
D-glycerate + CO2
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inducible by L-tartrate
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?
L-tartrate
D-glycerate + CO2
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best substrate
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?
L-tartrate
D-glycerate + CO2
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inducible by L-tartrate
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?
meso-tartrate
D-glycerate + CO2
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meso-tartrate
D-glycerate + CO2
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additional information
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not: D-tartrate, DL-malate
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additional information
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not: dihydroxyfumarate
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additional information
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not: dihydroxyfumarate
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additional information
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enzyme resembles L-tartrate dehydrogenase/D-malate dehydrogenase from Rhodopseudomonas sphaeroides and tartrate dehydrogenase from Pseudomonas putida, substrate specificity
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additional information
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not: D-tartrate, DL-malate
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additional information
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not: dihydroxyfumarate
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?
additional information
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not: dihydroxyfumarate
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additional information
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enzyme resembles L-tartrate dehydrogenase/D-malate dehydrogenase from Rhodopseudomonas sphaeroides and tartrate dehydrogenase from Pseudomonas putida, substrate specificity
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L-tartrate
D-glycerate + CO2
L-tartrate
D-glycerate + CO2
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inducible by L-tartrate
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?
L-tartrate
D-glycerate + CO2
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inducible by L-tartrate
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?
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NADP+
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requirement, less effective than NAD+
NAD+
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requirement
NAD+
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decarboxylation is not stoichiometrically related with NAD+, NAD+-reduction at 1.1% the rate of L-tartrate decarboxylation
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K+
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activation, above 40 mM
Mg2+
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activation
Mg2+
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optimum concentration is 0.2 mM
additional information
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not activated by Co2+ or Ca2+
additional information
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requirement of a divalent and a monovalent cation, not activated by Ca2+, Fe2+, Zn2+, Li+ or Na+
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D-glycerate
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product inhibition, 10 mM, 65% inhibition
D-malate
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10 mM, 83% inhibition
L-Glycerate
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10 mM, 63% inhibition
L-malate
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10 mM, 29% inhibition
meso-tartrate
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10 mM, 14% inhibition
succinate
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10 mM, 28% inhibition
EDTA
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1 mM, at 30°C, complete inhibition, 1 mM MgCl2 or MnCl2 reactivates
EDTA
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5 mM, at 30°C, complete inactivation
L-Tartrate
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1 mM/ml; strong substrate inhibition
L-Tartrate
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above 0.5 M; strong substrate inhibition
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7
L-Tartrate
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pH 7.5, 30°C
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5.5 - 9
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half-maximal activity at pH 5.5 and 9
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45
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D-glycerate formation with whole cells
30
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assay at
30
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optimum around and assay at
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4.9
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isoelectric focusing
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group Ve-2
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brenda
group Ve-2
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brenda
soil isolate
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brenda
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148000
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HPLC gel filtration
40000
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4 * 40000, SDS-PAGE
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homotetramer
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4 * 40000, SDS-PAGE
homotetramer
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4 * 40000, SDS-PAGE
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6.5
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30 min at 60°C, inactivation
648380
7
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30 min at 60°C, 23% loss of activity
648380
7.5
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30 min at 60°C, in 20 mM Tris-HCl buffer, 0.2 mM MgCl2, 5% loss of activity
648380
8
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30 min at 60°C, 13% loss of activity
648380
9
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30 min at 60°C, 57% loss of activity
648380
9.5
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30 min at 60°C, inactivation
648380
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50
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30 min, in 20 mM Tris-HCl buffer, pH 7.5, 0.2 mM MgCl2, stable
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30 min, in 20 mM Tris-HCl buffer, pH 7.5, 0.2 mM MgCl2, 5% loss of activity, inactivation at pH 6.5 and 9.5
65
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30 min, in 20 mM Tris-HCl buffer, pH 7.5, 0.2 mM MgCl2, 29% loss of activity
70
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30 min, in 20 mM Tris-HCl buffer, pH 7.5, 0.2 mM MgCl2, inactivation
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-20°C, 50% glycerol, 3 months, stable, without glycerol, 1 month, 40% loss of activity
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synthesis
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production of D-glycerate, which is a useful chiral synthon in synthetic organic chemistry
synthesis
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production of D-glycerate, which is a useful chiral synthon in synthetic organic chemistry
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Furuyoshi, S.; Kawabata, N.; Tanaka, H.; Soda, K.
Enzymic production of D-glycerate from L-tartrate
Agric. Biol. Chem.
53
2101-2105
1989
Pseudomonas sp., Pseudomonas sp. 5D1A
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brenda
Furuyoshi, S.; Nishigouri, J.; Kawabata, N.; Tanaka, H.; Soda, K.
D-Glycerate production from L-tartrate by cells of Pseudomonas sp. with high content of L-tartrate decarboxylase
Agric. Biol. Chem.
55
1515-1519
1991
Pseudomonas sp., Pseudomonas sp. 5D1A
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brenda
Furuyoshi, S.; Nawa, Y.; Kawabata, N.; Tanaka, H.; Soda, K.
Purification and characterization of a new NAD(+)-dependent enzyme, L-tartrate decarboxylase, from Pseudomonas sp. group Ve-2
J. Biochem.
110
520-525
1991
Pseudomonas sp., Pseudomonas sp. 5D1A
brenda
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4.1.1.73 tartrate decarboxylase
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