Information on EC 4.2.1.79 - 2-Methylcitrate dehydratase

New: Word Map on EC 4.2.1.79
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Mark a special word or phrase in this record:
Search Reference ID:
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)


The expected taxonomic range for this enzyme is: Bacteria, Eukaryota

EC NUMBER
COMMENTARY hide
4.2.1.79
-
RECOMMENDED NAME
GeneOntology No.
2-Methylcitrate dehydratase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
(2S,3S)-2-hydroxybutane-1,2,3-tricarboxylate = (Z)-but-2-ene-1,2,3-tricarboxylate + H2O
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
addition
-
-
double bond; of H2O to double bond
-
elimination of H2O
-
-
-
-
syn-elimination
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
2-methylcitrate cycle I
-
-
Propanoate metabolism
-
-
propionate fermentation
-
-
SYSTEMATIC NAME
IUBMB Comments
(2S,3S)-2-hydroxybutane-1,2,3-tricarboxylate hydro-lyase [(Z)-but-2-ene-1,2,3-tricarboxylate-forming]
The enzyme is specific for (2S,3S)-methylcitrate, showing no activity with (2R,3S)-methylcitrate [2]. The enzyme can also use cis-aconitate as a substrate but more slowly [2]. Both this enzyme and EC 4.2.1.3, aconitate hydratase, are required to complete the isomerization of (2S,3S)-methylcitrate to (2R,3S)-2-methylisocitrate [2].
CAS REGISTRY NUMBER
COMMENTARY hide
80891-26-5
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain M1
-
-
Manually annotated by BRENDA team
strain M1
-
-
Manually annotated by BRENDA team
strain B10
-
-
Manually annotated by BRENDA team
strain B10
-
-
Manually annotated by BRENDA team
gene acnD and prpF are both needed for full enzyme activity, they exist in place of or in addition to prpD
-
-
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
gene acnD and prpF are both needed for full enzyme activity, they exist in place of or in addition to prpD
-
-
Manually annotated by BRENDA team
formerly Saccaromycopsis lipolytica
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(2S,3S)-hydroxybutane-1,2,3-tricarboxylate
(Z)-but-2-ene-1,2,3-tricarboxylate + H2O
show the reaction diagram
(S)-malate
?
show the reaction diagram
-
-
-
?
(Z)-But-2-ene-1,2,3-tricarboxylate + H2O
2-Hydroxybutane-1,2,3-tricarboxylate
show the reaction diagram
2-Hydroxybutane-1,2,3-tricarboxylate
(Z)-But-2-ene-1,2,3-tricarboxylate + H2O
show the reaction diagram
2-Hydroxybutane-1,2,3-tricarboxylate
?
show the reaction diagram
-
methylcitric acid cycle, propionyl-CoA oxidation
-
-
-
2-methylcitrate
2-methyl-cis-aconitate + H2O
show the reaction diagram
cis-aconitate
?
show the reaction diagram
citrate
?
show the reaction diagram
citrate
cis-aconitate + H2O
show the reaction diagram
D-malate
?
show the reaction diagram
-
-
-
?
D-tartrate
?
show the reaction diagram
-
-
-
?
DL-citramalate
?
show the reaction diagram
-
-
-
?
DL-isocitrate
?
show the reaction diagram
-
-
-
?
L-tartrate
?
show the reaction diagram
-
-
-
?
meso-tartrate
?
show the reaction diagram
-
-
-
?
additional information
?
-
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
(2S,3S)-hydroxybutane-1,2,3-tricarboxylate
(Z)-but-2-ene-1,2,3-tricarboxylate + H2O
show the reaction diagram
P77243
enzyme performs the isomerization of (2S,3S)-methylcitrate to (2R,3S)-2-methylisocitrate together with aconitase, both enzymes are essential, overview
-
r
2-Hydroxybutane-1,2,3-tricarboxylate
(Z)-But-2-ene-1,2,3-tricarboxylate + H2O
show the reaction diagram
2-Hydroxybutane-1,2,3-tricarboxylate
?
show the reaction diagram
-
methylcitric acid cycle, propionyl-CoA oxidation
-
-
-
2-methylcitrate
2-methyl-cis-aconitate + H2O
show the reaction diagram
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
the enzyme contains no iron-sulfur center
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
no requirement for metal ions and reducing agents
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
citrate
-
competitive
DL-Fluorocitrate
-
competitive
iodoacetate
-
-
p-chloromercuribenzoate
-
-
threo-Isocitrate
-
competitive
-
tricarballylate
-
competitive
additional information
-
not: chelating agents
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Propionate
additional information
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.44
(2S,3S)-methylcitrate
-
0.19
2-Hydroxybutane-1,2,3-tricarboxylate
-
diastereomer
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.005
-
partially purified AcnC
0.2
purified recombinant His-tagged enzyme, substrate citrate
0.8
-
purified PrpD
2.6
purified recombinant His-tagged enzyme, substrate cis-aconitate
2.8
purified recombinant His-tagged enzyme, substrate 2-methylcitrate
additional information
-
substrate specificity
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7 - 8
-
for AcnC and PrpD
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.7
isoelectric focusing
5.8
-
isoelectric focusing
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
ORGANISM
UNIPROT
Escherichia coli (strain K12)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
78000 - 79000
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
purified recombinant His-tagged enzyme, 11.7 mg/ml, in 10 mM HEPES, pH 7.5, optimization of crystallization conditions with precipitant solution containing PEG or pentaerythriol propoxylate and pentaerythriol ethoxylate, overview, X-ray diffraction structure determination and analysis at beyond 2.0 A resolution
-
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5 - 7.5
-
-
5898
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40
-
30 min, stable
50
-
half-life is 30 min for both AcnC and PrpD
60
-
30 min, complete inactivation
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
unstable in Tris-HCl buffer
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
liquid N2, 0.05 M potassium phosphate buffer, pH 6.5, stable for more than 6 months
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
AcnC partially 0.25fold from AcnABnull strain, PrpD 14.3fold from overexpression in AcnABnull strain
-
recombinant His-tagged AcnD and PrpF from Escherichia coli BL21(DE3)
-
recombinant His-tagged enzyme from Escherichia coli BL21(DE3), to homogeneity
recombinant His-tagged enzyme from overexpressing strain
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination and analysis, genomic organization, expression of AcnC in AcnABnull strain, overexpression of PrpD in AcnABnull strain
-
expression of His-tagged AcnD and PrpF in Escherichia coli BL21(DE3), functional complementation of an enzyme-deficient mutant of Salmonella enterica only by expression of both AcnD and PrpF
-
gene prpD in the operon prpBCDE, DNA sequence determination nand analysis, overexpression as N-terminally His-tagged protein in Escherichia coli BL21(DE3)
genomic structure of prp operon, expression studies in Escherichia coli K12 strain W3350, and overexpression of the N-terminally His-tagged enzyme
structural genetic organization of prp operon
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
2-methylcitrate dehydratase is induced 3.6fold by treatment with Ag+, no induction by Co2+
Show AA Sequence (1766 entries)
Please use the Sequence Search for a certain query.