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Information on EC 4.2.1.79 - 2-methylcitrate dehydratase and Organism(s) Escherichia coli and UniProt Accession P77243
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4.2.1.79 2-methylcitrate dehydrataseIUBMB Comments
The enzyme is specific for (2S,3S)-methylcitrate, showing no activity with (2R,3S)-methylcitrate . The enzyme can also use cis-aconitate as a substrate but more slowly . 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 .
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Word Map
- 4.2.1.79
- propionate
- propionyl-coa
- enterica
- isocitrate
- tuberculosis
- methylisocitrate
- oneidensis
- cis-aconitate
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prpbcde
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odd-chain
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shewanella
- glyoxylate
- prpf
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beta-oxidation
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serovar
- smegmatis
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propionyl
The taxonomic range for the selected organisms is: Escherichia coli
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Reaction Schemes
Synonyms
2-methylcitrate dehydratase, methylcitrate dehydratase, seprpd, 2-mc dehydratase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
2-Methylcitrate hydro-lyase
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Dehydratase, 2-methylcitrate
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-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
elimination of H2O
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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
80891-26-5
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(2S,3S)-2-hydroxybutane-1,2,3-tricarboxylate
(E)-but-2-ene-1,2,3-tricarboxylate + H2O
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-
-
?
(2S,3S)-2-hydroxybutane-1,2,3-tricarboxylate
(Z)-but-2-ene-1,2,3-tricarboxylate + H2O
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-
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?
cis-aconitate
?
5fold lower activity than with 2-methylcitrate
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?
(2S,3S)-2-methylcitrate
cis-2-methylaconitate
the enzyme is involved in the methylcitric acid cycle
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-
?
(2S,3S)-2-methylcitrate
cis-2-methylaconitate
the MmgE enzyme is not a stereospecific 2-methylcitrate dehydratase because it can dehydrate at least two of the four diastereomers of 2-methylcitrate to yield either (E)-2-methylaconitate or (Z)-2-methylaconitate
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-
?
(2S,3S)-hydroxybutane-1,2,3-tricarboxylate
(Z)-but-2-ene-1,2,3-tricarboxylate + H2O
i.e. 2-methylcitrate, highly specific for, stereospecific for (2S,3S)-methylcitrate, the reverse reaction is an unusual syn-elimination
i.e. 2-methyl-cis-aconitate
?
(2S,3S)-hydroxybutane-1,2,3-tricarboxylate
(Z)-but-2-ene-1,2,3-tricarboxylate + H2O
enzyme performs the isomerization of (2S,3S)-methylcitrate to (2R,3S)-2-methylisocitrate together with aconitase, both enzymes are essential, overview
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r
2-Hydroxybutane-1,2,3-tricarboxylate
(Z)-But-2-ene-1,2,3-tricarboxylate + H2O
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i.e. 2-methylcitrate, best substrate
i.e. 2-methyl-cis-aconitate
?
2-Hydroxybutane-1,2,3-tricarboxylate
(Z)-But-2-ene-1,2,3-tricarboxylate + H2O
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metabolic function
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?
additional information
?
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(2R,3S)-isocitrate and citrate are poor substrates, no activity with trans-aconitate, threo-2-methylisocitrate, erythro-2-methylisocitrate, (S)-malate and (R)-malate
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?
additional information
?
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(2R,3S)-isocitrate and citrate are poor substrates, no activity with trans-aconitate, threo-2-methylisocitrate, erythro-2-methylisocitrate, (S)-malate and (R)-malate
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?
additional information
?
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the PrpD enzyme from Escherichia coli is not a stereospecific 2-methylcitrate dehydratase because it can dehydrate at least two of the four diastereomers of 2-methylcitrate to yield either (E)-2-methylaconitate or (Z)-2-methylaconitate, but the physiological pathways proceed via (Z)-2-methylaconitate, which serves as the substrate for the citB enzyme in the synthesis of 2-methylisocitrate
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?
additional information
?
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substrate specificity, no activity with cis-aconitate and related substances containing double bonds, overview
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?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(2S,3S)-2-hydroxybutane-1,2,3-tricarboxylate
(Z)-but-2-ene-1,2,3-tricarboxylate + H2O
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-
-
?
(2S,3S)-2-methylcitrate
cis-2-methylaconitate
the enzyme is involved in the methylcitric acid cycle
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-
?
(2S,3S)-hydroxybutane-1,2,3-tricarboxylate
(Z)-but-2-ene-1,2,3-tricarboxylate + H2O
enzyme performs the isomerization of (2S,3S)-methylcitrate to (2R,3S)-2-methylisocitrate together with aconitase, both enzymes are essential, overview
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r
2-Hydroxybutane-1,2,3-tricarboxylate
(Z)-But-2-ene-1,2,3-tricarboxylate + H2O
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metabolic function
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?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Fe2+
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enzyme possesses 1 unstable iron-sulfur center per monomer, required for activity, can be reconstituted by Fe2+ under reducing conditions
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
gene prpD, part of the prp operon, induction and expression depends on propionate during growth
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additional information
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gene prpD, part of the prp operon, induction and expression depends on propionate during growth
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
gene prpD, part of the prp operon, induction and expression depends on propionate during growth
SwissProt
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
physiological function
the PrpD enzyme from Escherichia coli is not a stereospecific 2-methylcitrate dehydratase because it can dehydrate at least two of the four diastereomers of 2-methylcitrate to yield either (E)-2-methylaconitate or (Z)-2-methylaconitate, but the physiological pathways proceed via (Z)-2-methylaconitate, which serves as the substrate for the citB enzyme in the synthesis of 2-methylisocitrate
metabolism
the enzyme is involved in the 2-methylcitric acid cycle, overview
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
AcnC partially 0.25fold from AcnABnull strain, PrpD 14.3fold from overexpression in AcnABnull strain
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene prpD, the mother cell metabolic gene (mmg) operon encodes homologues from the methylcitric acid cycle
genomic structure of prp operon, expression studies in Escherichia coli K12 strain W3350, and overexpression of the N-terminally His-tagged enzyme
DNA and amino acid sequence determination and analysis, genomic organization, expression of AcnC in AcnABnull strain, overexpression of PrpD in AcnABnull strain
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Brock, M.; Maerker, C.; Schuetz, A.; Voelker, U.; Buckel, W.
Oxidation of propionate to pyruvate in Escherichia coli: Involvement of methylcitrate dehydratase and aconitase
Eur. J. Biochem.
269
6184-6194
2002
Escherichia coli (P77243), Escherichia coli
Blank, L.; Green, J.; Guest, J.R.
AcnC of Escherichia coli is a 2-methylcitrate dehydratase (PrpD) that can use citrate and isocitrate as substrates
Microbiology
148
133-146
2002
Escherichia coli
Reddick, J.J.; Sirkisoon, S.; Dahal, R.A.; Hardesty, G.; Hage, N.E.; Booth, W.T.; Quattlebaum, A.L.; Mills, S.N.; Meadows, V.G.; Adams, S.L.H.; Doyle, J.S.; Kiel, B.E.
First biochemical characterization of a methylcitric acid cycle from Bacillus subtilis strain 168
Biochemistry
56
5698-5711
2017
Bacillus subtilis (P45859), Bacillus subtilis 168 (P45859), Escherichia coli (P77243), Escherichia coli, Escherichia coli K12 (P77243)
Rocco, C.J.; Wetterhorn, K.M.; Garvey, G.S.; Rayment, I.; Escalante-Semerena, J.C.
The PrpF protein of Shewanella oneidensis MR-1 catalyzes the isomerization of 2-methyl-cis-aconitate during the catabolism of propionate via the AcnD-dependent 2-methylcitric acid cycle
PLoS ONE
12
e0188130
2017
Bacillus subtilis (P45859), Bacillus subtilis 168 (P45859), Escherichia coli (P77243), Salmonella enterica subsp. enterica serovar Typhimurium (P74840), Salmonella enterica subsp. enterica serovar Typhimurium LT2 / SGSC1412 / ATCC 700720 (P74840)
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