Information on EC 1.14.20.3 - (5R)-carbapenem-3-carboxylate synthase

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The expected taxonomic range for this enzyme is: Pectobacterium carotovorum

EC NUMBER
COMMENTARY hide
1.14.20.3
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RECOMMENDED NAME
GeneOntology No.
(5R)-carbapenem-3-carboxylate synthase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
(3S,5S)-carbapenam-3-carboxylate + 2-oxoglutarate + O2 = (5R)-carbapen-2-em-3-carboxylate + succinate + CO2 + H2O
show the reaction diagram
(3S,5S)-carbapenam-3-carboxylate + 2-oxoglutarate + O2 = (5R)-carbapenem-3-carboxylate + succinate + CO2 + H2O
show the reaction diagram
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
(5R)-carbapenem carboxylate biosynthesis
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Carbapenem biosynthesis
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Biosynthesis of antibiotics
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SYSTEMATIC NAME
IUBMB Comments
(3S,5S)-carbapenam-3-carboxylate,2-oxoglutarate:oxygen oxidoreductase (dehydrating)
Requires Fe2+. The enzyme is involved in the biosynthesis of the carbapenem beta-lactam antibiotic (5R)-carbapen-2-em-3-carboxylate in the bacterium Pectobacterium carotovorum. It catalyses a stereoinversion at C-5 and introduces a double bond between C-2 and C-3.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(3R,5R)-carbapenam-3-carboxylate + 2-oxoglutarate + O2
(5R)-carbapen-2-em-3-carboxylate + succinate + CO2 + H2O
show the reaction diagram
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activity in presence of ascorbate is 22% compared to the activity with the natural substrate (3S,5S)-carbapenam-3-carboxylate, activity in absence of ascorbate is 86% compared to the activity with the natural substrate (3S,5S)-carbapenam-3-carboxylate in presence of ascorbate
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-
?
(3R,5S)-carbapenam-3-carboxylate + 2-oxoglutarate + O2
(5R)-carbapen-2-em-3-carboxylate + succinate + CO2 + H2O
show the reaction diagram
-
activity in presence of ascorbate is less than 2% compared to the activity with the natural substrate (3S,5S)-carbapenam, activity in absence of ascorbate is 40% compared to the activity with the natural substrate (3S,5S)-carbapenam in presence of ascorbate
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-
?
(3S,5R)-carbapenam-3-carboxylate + 2-oxoglutarate + O2
(5R)-carbapen-2-em-3-carboxylate + succinate + CO2 + H2O
show the reaction diagram
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activity in presence of ascorbate is 76% compared to the activity with the natural substrate (3S,5S)-carbapenam-3-carboxylate, activity in absence of ascorbate is 7% compared to the activity with the natural substrate (3S,5S)-carbapenam-3-carboxylate in presence of ascorbate
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-
?
(3S,5S)-carbapen-2-am-3-carboxylate + 2-oxoglutarate + O2
(5R)-carbapen-2-em-3-carboxylate + succinate + CO2 + H2O
show the reaction diagram
(3S,5S)-carbapenam-3-carboxylate + 2-oxoglutarate + O2
(5R)-carbapen-2-em-3-carboxylate + succinate + CO2 + H2O
show the reaction diagram
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
(3S,5S)-carbapen-2-am-3-carboxylate + 2-oxoglutarate + O2
(5R)-carbapen-2-em-3-carboxylate + succinate + CO2 + H2O
show the reaction diagram
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the enzyme is involved in the biosynthesis of (5R)-carbapen-2-em-3-carboxylic acid the simplest structurally among the naturally occurring carbapenem beta-lactam antibiotics
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?
(3S,5S)-carbapenam-3-carboxylate + 2-oxoglutarate + O2
(5R)-carbapen-2-em-3-carboxylate + succinate + CO2 + H2O
show the reaction diagram
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?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Fe2+
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required for activity
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ascorbate
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activity with the natural substrate (3S,5S)-carbapenam-3-carboxylate in absence of ascorbate is 2% compared to the activity in presence of ascorbate. Ascorbate does not stimulate turnover of the (3S,5R)- or (3R,5R)-stereoisomers
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
200000
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hexamer
CarC crystallizes as a hexamer comprised of two trimers. Predominant form of CarC in solution is also hexameric with low levels of monomeric and trimeric forms also being observed
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
hanging-drop vapor diffusion method. Crystal structures of CarC complexed with Fe(II) and 2-oxoglutarate reveal it to be hexameric (space group C2221), consistent with solution studies. CarC monomers contain a double-stranded beta-helix core that supports ligands binding a single Fe(II) to which 2-oxoglutarate complexes in a bi-dentate manner. A structure is obtained with L-N-acetylproline acting as a substrate analogue. Quantum mechanical/molecular mechanical modeling studies with stereoisomers of carbapenams and carbapenems are used to investigate substrate binding
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
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expression in Escherichia coli BL21