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Information on EC 4.2.1.32 - L(+)-tartrate dehydratase
for references in articles please use BRENDA:EC4.2.1.32
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IUBMB Comments
The enzyme exists in an inactive low-molecular-mass form, which is converted into active enzyme in the presence of Fe2+ and thiol. cf. EC 4.2.1.81 D(-)-tartrate dehydratase.
The expected taxonomic range for this enzyme is: Bacteria, Archaea
- 4.2.1.32
- succinate
- d-tartrate
-
antiporter
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c4-dicarboxylate
- fumarase
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stereoisomer
- meso-tartrate
- beta-subunits
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lysr-type
showSynonyms
l-tartrate dehydratase, tartrate dehydratase, l-ttd, l(+)-tartrate dehydratase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Dehydratase, tartrate
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L-(+)-Tartaric acid dehydrase
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-
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L-(+)-Tartrate dehydratase
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-
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L-Tartrate dehydratase
L-Ttd
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L-TTD alpha
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L-TTD beta
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Tartaric acid dehydrase
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-
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Tartrate dehydratase
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additional information
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meso-tartrate dehydratase, similar enzyme, specific for meso-tartrate
L-Tartrate dehydratase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
(R,R)-Tartrate = oxaloacetate + H2O
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
elimination
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
(R,R)-tartrate hydro-lyase (oxaloacetate-forming)
The enzyme exists in an inactive low-molecular-mass form, which is converted into active enzyme in the presence of Fe2+ and thiol. cf. EC 4.2.1.81 D(-)-tartrate dehydratase.
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CAS REGISTRY NUMBER
COMMENTARY
9014-40-8
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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
L-tartrate
oxaloacetate + H2O
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Substrates: anaerobic growth of Escherichia coli on D-tartrate depends on the fumarate carrier DcuB and fumarase, rather than the L-tartrate carrier TtdT and L-tartrate dehydratase
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(R,S)-Tartrate
Oxaloacetate + H2O
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Substrates: in the presence of glycerol and (R,S)-tartrate under anaerobic conditions
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(R,S)-Tartrate
Oxaloacetate + H2O
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Substrates: no activity with D-(-)-tartrate, (R,S)-tartrate
Products: -
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L-(+)-Tartrate
Oxaloacetate + H2O
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Substrates: in the presence of glycerol (R,R)-tartrate can be used as reducible substrate for supporting anaerobic growth
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L-(+)-Tartrate
Oxaloacetate + H2O
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Substrates: no activity with D-(-)-tartrate, (R,S)-tartrate
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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
L-tartrate
oxaloacetate + H2O
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Substrates: anaerobic growth of Escherichia coli on D-tartrate depends on the fumarate carrier DcuB and fumarase, rather than the L-tartrate carrier TtdT and L-tartrate dehydratase
Products: -
Products: -
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Fe2+
additional information
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requirement for Fe2+ cannot be replaced by Mg2+, Ba2+, Mn2+, Co2+, Ni2+, Zn2+, Cu2+, Al3+, BO32-, MoO42- at concentrations of 0.01 mM and 1 mM
Fe2+
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addition of either GSH or cysteine plus Fe2+ reactivates inactive enzyme, optimum Fe2+ concentration 1 mM, Fe2+ only required for activation
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2.1
(R,R)-Tartrate
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both, under anaerobic conditions and in the presence of air
additional information
additional information
-
reducing conditions: 2 KM-values/biphasic curve, presence of air: only one higher KM-value obtained
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additional information
additional information
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reducing conditions: 2 KM-values/biphasic curve, presence of air: only one higher KM-value obtained
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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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pH RANGE
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 Links Show AA Sequence and Transmembrane Helices (2158 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
145000
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sucrose density gradient centrifugation, active form. Enzyme exists as an aggregate of smaller protein or proteins, the latter possessing no enzyme activity
22641
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2 * 22641 + 2 * 32589, DNA-derived values of TtdB and TtdA, quaternary structure of Escherichia coli K12 (W3110, wild-type) resembles that of the Pseudomonas putida enzyme
32589
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2 * 22641 + 2 * 32589, DNA-derived values of TtdB and TtdA, quaternary structure of Escherichia coli K12 (W3110, wild-type) resembles that of the Pseudomonas putida enzyme
39000
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sucrose density gradient centrifugation, inactive form. Aggregation of the four smaller units forms the active protein
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
tetramer
monomer
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1 * 39000 sucrose density gradient centrifugation, inactive form, activation by aggregation of 4 monomeres
tetramer
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2 * 22641 + 2 * 32589, DNA-derived values of TtdB and TtdA, quaternary structure of Escherichia coli K12 (W3110, wild-type) resembles that of the Pseudomonas putida enzyme
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
cell extracts are prepared in extraction buffer and maintain at 0°C under N2 for more than 1 h before assaying for enzyme activity
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crude cell-extract completely loses activity in open tubes in ice bath for 2-4 h, activity restored after incubation at 25°C for 30 min, extent of activation decreases with each succeeding cycle of inactivation and reactivation, loss of activity after treatment with EDTA or after dialysis
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Cysteine 100 mM Cysteine plus 1 mM Fe2+ optimal reactivation of inactive enzyme
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equimolar mixture of 50 mM GSH and 50 mM Cysteine plus 1 mM Fe2+ optimum reactivation of inactive enzyme
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manipulations on dye-ligand columns cause rapid irrecoverable loss of activity
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OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
reactivation of the inactive enzyme is seriously inhibited by exposure to air
-
5653
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, under reduced pressure and minimized contact with air several months
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
expression of plasmid-encoded ttdA'-'lacZ is stimulated to a high level (64fold) by L-tartrate during anaerobic growth. meso-Tartrate causes slightly lower (47.5fold) induction. During aerobic growth, expression of ttdA'-'lacZ is very low in the presence or absence of L-tartrate, and it increases by a factor of about 220 under anaerobic conditions. Expression of ttdA requires transcriptional activation by fumarate nitrate reductase regulator (FNR), which is in the active state only under anaerobic conditions
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expression of ttdA is repressed by O2 in an FNR-dependent manner. Presence of nitrate strongly represses ttdA. When glucose is present in addition to L-tartrate, expression of ttdA'-'lacZ is decreased to 24% of the L-tartrate-induced state
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Hurlbert, R.E.; Jakoby, W.B.
L-(+)-Tartaric acid dehydrase
Methods Enzymol.
9
680-682
1966
Pseudomonas putida
-
brenda
Furuyoshi, S.; Tanaka, H.; Soda, K.
Occurrence of a New Enzyme, meso-Tartrate Dehydratase of Pseudomonas putida
Agric. Biol. Chem.
51
1495-1499
1987
Pseudomonas putida
-
brenda
Hurlbert, R.E.; Jakoby, W.B.
Tartaric acid metabolism
J. Biol. Chem.
240
2772-2777
1965
Pseudomonas putida
brenda
Kelly, J.M.; Scopes, R.K.
L-(+)-Tartrate dehydratase from Pseudomonas putida is an iron-sulphur enzyme
FEBS Lett.
202
274-276
1986
Pseudomonas putida
-
brenda
Schink, B.
Fermentation of tartrate enantiomers by anaerobic bacteria, and description of two new species of strict anaerobes Ruminococcus pasteurii and Ilyobacter tartaricus
Arch. Microbiol.
139
409-414
1984
Acetivibrio sp., Bacteria, Bacteroides sp., Ilyobacter sp., Ilyobacter tartaricus, Trichococcus pasteurii
-
brenda
Reaney, S.K.; Begg, C.; Bungard, S.J.; Guest J.R.
Identification of the L-tartrate dehydratase genes (ttdA and ttdB) of Escherichia coli and evolutioary relationship with the Class I fumarase genes
J. Gen. Microbiol.
139
1523-1530
1993
Escherichia coli
brenda
Yashphe, J.; Rosenberger, R.F.; Shilo, M.; Schwartz, L.
The loss of meso-tartrate dehydratase activity from induced cells of Pseudomonas
Biochim. Biophys. Acta
146
560-576
1967
Pseudomonas sp.
brenda
Kim, O.B.; Lux, S.; Unden, G.
Anaerobic growth of Escherichia coli on D-tartrate depends on the fumarate carrier DcuB and fumarase, rather than the L-tartrate carrier TtdT and L-tartrate dehydratase
Arch. Microbiol.
188
583-589
2007
Escherichia coli
brenda
Kim, O.B.; Reimann, J.; Lukas, H.; Schumacher, U.; Grimpo, J.; Duennwald, P.; Unden, G.
Regulation of tartrate metabolism by TtdR and relation to the DcuS-DcuR-regulated C4-dicarboxylate metabolism of Escherichia coli
Microbiology
155
3632-3640
2009
Escherichia coli
brenda
EXTERNAL LINKS (specific for EC-Number 4.2.1.32)
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Release 2023.1 (January 2023)
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