6.3.3.6: carbapenam-3-carboxylate synthase
This is an abbreviated version!
For detailed information about carbapenam-3-carboxylate synthase, go to the full flat file.
Word Map on EC 6.3.3.6
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6.3.3.6
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carbapenams
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beta-lactamization
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simplest
-
monocyclic
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crotonase
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malonyl-coa
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bicyclic
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stereoselective
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beta-ls
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asparagine
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ph-rate
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biocatalytic
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synthases
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viscosity
-
synthesis
- 6.3.3.6
-
carbapenams
-
beta-lactamization
-
simplest
-
monocyclic
- crotonase
- malonyl-coa
-
bicyclic
-
stereoselective
-
beta-ls
- asparagine
-
ph-rate
-
biocatalytic
- synthases
-
viscosity
- synthesis
Reaction
Synonyms
CarA, carbapenam 3-carboxylate synthase, carbapenam synthetase, CPS, EC 6.3.1.16
ECTree
6.3.3.6 carbapenam-3-carboxylate synthaseAdvanced search results
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results (Engineering
Engineering on EC 6.3.3.6 - carbapenam-3-carboxylate synthase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
E380D
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retains a functional general base with a pKa of about 7.4 for kcat. The acidic region of the log (kcat/Km) versus pH profiles displays an ionizable group with a pKa of about 7.7. kcat/Km is 1.4fold lower compared to wild-type value
E380Q
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variant displays a plateau in the acidic region. The acidic region of the log (kcat/Km) versus pH profiles becomes pH-independent for E380Q. kcat/Km is 3.8fold lower compared to wild-type value
K443A
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at pH 8.0, 6.33 and 9.33 the mutant enzyme shows no measurable activity
K443M
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at pH 8.0, 6.33 and 9.33 the mutant enzyme shows no measurable activity
Y345A
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mutant exhibits a 5fold increase in Km of (2S,5S)-5-carboxymethylproline and a 165fold decrease in specificity constant compared to wild-type enzyme. kcat/Km is 165fold lower compared to wild-type value
Y345F
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pH-dependent kcat and kcat/Km plots retain the bell-shaped curve of wild-type CPS with similar pK values. kcat/Km is 1.7fold lower compared to wild-type value
