Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 1.14.20.3 - (5R)-carbapenem-3-carboxylate synthase and Organism(s) Pectobacterium carotovorum and UniProt Accession Q9XB59

for references in articles please use BRENDA:EC1.14.20.3
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
IUBMB Comments
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.
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Pectobacterium carotovorum
UNIPROT: Q9XB59
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
  • 1.14.20.3
  • epimerization
  • desaturation
  • oxygenase
  • carbapenams
  • bicyclic
  • biosynthesized
  • donate
The taxonomic range for the selected organisms is: Pectobacterium carotovorum
The enzyme appears in selected viruses and cellular organisms
Synonyms
carbapenem synthase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
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.
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
-
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
-
-
?
(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
-
-
?
(3S,5R)-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 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
-
-
?
(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 SUBSTRATE
NATURAL PRODUCT
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
-
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
-
-
?
(3S,5S)-carbapenam-3-carboxylate + 2-oxoglutarate + O2
(5R)-carbapen-2-em-3-carboxylate + succinate + CO2 + H2O
show the reaction diagram
-
-
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Fe2+
-
required for activity
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ascorbate
-
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
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
200000
gel filtration
SUBUNIT
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 BL21
expression in Escherichia coli
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Sleeman, M.C.; Smith, P.; Kellam, B.; Chhabra, S.R.; Bycroft, B.W.; Schofield, C.J.
Biosynthesis of carbapenem antibiotics: new carbapenam substrates for carbapenem synthase (CarC)
Chembiochem
5
879-882
2004
Pectobacterium carotovorum
Manually annotated by BRENDA team
Stapon, A.; Li, R.; Townsend, C.A.
Synthesis of (3S,5R)-carbapenam-3-carboxylic acid and its role in carbapenem biosynthesis and the stereoinversion problem
J. Am. Chem. Soc.
125
15746-15747
2003
Pectobacterium carotovorum
Manually annotated by BRENDA team
Stapon, A.; Li, R.; Townsend, C.A.
Carbapenem biosynthesis: confirmation of stereochemical assignments and the role of CarC in the ring stereoinversion process from L-proline
J. Am. Chem. Soc.
125
8486-8493
2003
Pectobacterium carotovorum
Manually annotated by BRENDA team
Topf, M.; Sandala, G.M.; Smith, D.M.; Schofield, C.J.; Easton, C.J.; Radom, L.
The unusual bifunctional catalysis of epimerization and desaturation by carbapenem synthase
J. Am. Chem. Soc.
126
9932-9933
2004
Pectobacterium carotovorum
Manually annotated by BRENDA team
Clifton, I.J.; Doan, L.X.; Sleeman, M.C.; Topf, M.; Suzuki, H.; Wilmouth, R.C.; Schofield, C.J.
Crystal structure of carbapenem synthase (CarC)
J. Biol. Chem.
278
20843-20850
2003
Pectobacterium carotovorum (Q9XB59)
Manually annotated by BRENDA team
Borowski, T.; Broclawik, E.; Schofield, C.J.; Siegbahn, P.E.
Epimerization and desaturation by carbapenem synthase (CarC). A hybrid DFT study
J. Comput. Chem.
27
740-748
2006
Pectobacterium carotovorum
Manually annotated by BRENDA team
McGowan, S.J.; Sebaihia, M.; Porter, L.E.; Stewart, G.S.; Williams, P.; Bycroft, B.W.; Salmond, G.P.
Analysis of bacterial carbapenem antibiotic production genes reveals a novel beta-lactam biosynthesis pathway
Mol. Microbiol.
22
415-426
1996
Pectobacterium carotovorum
Manually annotated by BRENDA team