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Information on EC 4.1.3.30 - Methylisocitrate lyase and Organism(s) Escherichia coli and UniProt Accession P77541

for references in articles please use BRENDA:EC4.1.3.30
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EC Tree
     4 Lyases
         4.1 Carbon-carbon lyases
             4.1.3 Oxo-acid-lyases
                4.1.3.30 Methylisocitrate lyase
IUBMB Comments
The enzyme acts on threo-Ds-2-methylisocitrate, but not on threo-Ds-isocitrate, threo-DL-isocitrate or erythro-Ls-isocitrate.
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This record set is specific for:
Escherichia coli
UNIPROT: P77541
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Word Map
The taxonomic range for the selected organisms is: Escherichia coli
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
2-methylisocitrate lyase, methylisocitrate lyase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2-Methylisocitrate lyase
-
-
-
-
Lyase, methylisocitrate
-
-
-
-
MICL
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -
SYSTEMATIC NAME
IUBMB Comments
(2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate pyruvate-lyase (succinate-forming)
The enzyme acts on threo-Ds-2-methylisocitrate, but not on threo-Ds-isocitrate, threo-DL-isocitrate or erythro-Ls-isocitrate.
CAS REGISTRY NUMBER
COMMENTARY hide
57827-77-7
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(2S,3R)-3-Hydroxybutane-1,2,3-tricarboxylate
Pyruvate + succinate
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
dependent
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.024
(2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
19
(2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystals of the inactive mutant C123S MICL in complex with isocitrate are obtained at room temperature by vapor diffusion in hanging drops. A crystal of C123S MICL in complex with pyruvate and succinate was obtained by overnight incubation of a C123S MICL/isocitrate complex crystal in a solution containing 35% PEG3350, 100 mM pyruvate and 100 mM succinate. This crystal also belongs to space group C2
sitting drop vapor diffusion method
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Grimm, C.; Evers, A.; Brock, M.; Maerker, C.; Klebe, G.; Buckel, W.; Reuter, K.
Crystal structure of 2-methylisocitrate lyase (PrpB) from Escherichia coli and modelling of its ligand bound active centre
J. Mol. Biol.
328
609-621
2003
Escherichia coli (P77541), Escherichia coli
Manually annotated by BRENDA team
Liu, S.; Lu, Z.; Han, Y.; Melamud, E.; Dunaway-Mariano, D.; Herzberg, O.
Crystal structures of 2-methylisocitrate lyase in complex with product and with isocitrate inhibitor provide insight into lyase substrate specificity, catalysis and evolution
Biochemistry
44
2949-2962
2005
Escherichia coli (P77541)
Manually annotated by BRENDA team