Information on EC 4.2.1.32 - L(+)-Tartrate dehydratase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
4.2.1.32
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RECOMMENDED NAME
GeneOntology No.
L(+)-Tartrate dehydratase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
(R,R)-Tartrate = oxaloacetate + H2O
show the reaction diagram
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
elimination
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Glyoxylate and dicarboxylate metabolism
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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.
CAS REGISTRY NUMBER
COMMENTARY hide
9014-40-8
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Acetivibrio sp.
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-
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Manually annotated by BRENDA team
anaerobic
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Manually annotated by BRENDA team
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-
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Manually annotated by BRENDA team
Ilyobacter sp.
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Manually annotated by BRENDA team
GraTa2, DSM 2382
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
KoTa2, DSM 2381
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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,R)-Tartrate
?
show the reaction diagram
(R,S)-Tartrate
Oxaloacetate + H2O
show the reaction diagram
L-(+)-Tartrate
Oxaloacetate + H2O
show the reaction diagram
L-tartrate
oxaloacetate + H2O
show the reaction diagram
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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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?
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
(R,R)-Tartrate
?
show the reaction diagram
L-tartrate
oxaloacetate + H2O
show the reaction diagram
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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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?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(R,S)-tartrate
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competitive
cysteine
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35% inhibition at 50 mM
D-malic acid
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K-salt of
glutathione
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13% inhibition at 50 mM
L-Malic acid
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K-salt of
L-threonic acid
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K-salt of
Tartronic acid
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.76 - 2.1
(R,R)-Tartrate
additional information
additional information
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.6 - 9.4
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50% of maximal activity at pH 7.6 and at pH 9.4
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25
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assay at
PDB
SCOP
CATH
ORGANISM
UNIPROT
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
23000
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2 * 23000 + 2 * 27000, SDS-PAGE
27000
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2 * 23000 + 2 * 27000, SDS-PAGE
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
100000
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gel filtration
105000
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gel filtration
110500
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DNA-derived values of TtdA and TtdB
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
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
tetramer
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
100 mM GSH plus 1mM Fe2+ optimal reactivation of inactive enzyme
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cell extracts are prepared in extraction buffer and maintain at 0C 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 25C 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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no significant loss of activity after repeated freezing and thawing
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sucrose and/or succinate stabilize
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OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
oxygen-labile
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5656
reactivation of the inactive enzyme is seriously inhibited by exposure to air
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5653
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, cell-extracts in air 90% loss of activity in less than 10 h
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-20C, under reduced pressure and minimized contact with air several months
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression of plasmid-encoded ttdA'-'lacZ
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overexpressed in DH5 alpha (pGS581)
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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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