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Enzyme Nomenclature
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
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EC NUMBER 
COMMENTARY 
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
ORGANISM
UNIPROT
LITERATURE
(3S,5S)-carbapenam-3-carboxylate + 2-oxoglutarate + O2 = (5R)-carbapen-2-em-3-carboxylate + succinate + CO2 + H2O
(3S,5S)-carbapenam-3-carboxylate + 2-oxoglutarate + O2 = (5R)-carbapenem-3-carboxylate + succinate + CO2 + H2O
(3S,5S)-carbapenam-3-carboxylate + 2-oxoglutarate + O2 = (5R)-carbapen-2-em-3-carboxylate + succinate + CO2 + H2O
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(3S,5S)-carbapenam-3-carboxylate + 2-oxoglutarate + O2 = (5R)-carbapen-2-em-3-carboxylate + succinate + CO2 + H2O
the contrathermodynamic epimerization of (3S,5S)-carbapenam-3-carboxylate to (3S,5R)-carbapenam-3-carboxylate is coupled at least to the binding of 2-oxoglutarate and it is probably coupled to the reduction of molecular oxygen and proceeds by way of radical abstraction at C-5. The presumed Fe(IV)=O species formed in these processes is required to drive the subsequent desaturation process
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(3S,5S)-carbapenam-3-carboxylate + 2-oxoglutarate + O2 = (5R)-carbapen-2-em-3-carboxylate + succinate + CO2 + H2O
mechanism
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(3S,5S)-carbapenam-3-carboxylate + 2-oxoglutarate + O2 = (5R)-carbapenem-3-carboxylate + succinate + CO2 + H2O
a mechanism for CarC-catalyzed coupled epimerization and desaturation reactions is proposed
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(3S,5S)-carbapenam-3-carboxylate + 2-oxoglutarate + O2 = (5R)-carbapenem-3-carboxylate + succinate + CO2 + H2O
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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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.
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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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
(3R,5R)-carbapenam-3-carboxylate + 2-oxoglutarate + O2
(5R)-carbapen-2-em-3-carboxylate + succinate + CO2 + H2O
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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
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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
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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
(3S,5S)-carbapenam-3-carboxylate + 2-oxoglutarate + O2
(5R)-carbapen-2-em-3-carboxylate + succinate + CO2 + H2O
(3S,5S)-carbapen-2-am-3-carboxylate + 2-oxoglutarate + O2
(5R)-carbapen-2-em-3-carboxylate + succinate + CO2 + H2O
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(3S,5S)-carbapen-2-am-3-carboxylate + 2-oxoglutarate + O2
(5R)-carbapen-2-em-3-carboxylate + succinate + CO2 + H2O
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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
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-
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-
?
(3S,5S)-carbapenam-3-carboxylate + 2-oxoglutarate + O2
(5R)-carbapen-2-em-3-carboxylate + succinate + CO2 + H2O
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natural substrate. Activity with in absence of ascorbate is 2% compared to the activity in presence of ascorbate
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?
(3S,5S)-carbapenam-3-carboxylate + 2-oxoglutarate + O2
(5R)-carbapen-2-em-3-carboxylate + succinate + CO2 + H2O
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the contrathermodynamic epimerization of (3S,5S)-carbapenam-3-carboxylate to (3S,5R)-carbapenam-3-carboxylate is coupled at least to the binding of 2-oxoglutarate and it is probably coupled to the reduction of molecular oxygen and proceeds by way of radical abstraction at C-5. The presumed Fe(IV)=O species formed in these processes is required to drive the subsequent desaturation process
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?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
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
(3S,5S)-carbapen-2-am-3-carboxylate + 2-oxoglutarate + O2
(5R)-carbapen-2-em-3-carboxylate + succinate + CO2 + H2O
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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
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?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
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
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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PDB
SCOP
CATH
ORGANISM
UNIPROT
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
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
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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
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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LINKS TO OTHER DATABASES (specific for EC-Number 1.14.20.3)
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