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Literature summary extracted from

  • Raber, M.L.; Arnett, S.O.; Townsend, C.A.
    A conserved tyrosyl-glutamyl catalytic dyad in evolutionarily linked enzymes: carbapenam synthetase and beta-lactam synthetase (2009), Biochemistry, 48, 4959-40971.
    View publication on PubMedView publication on EuropePMC

Protein Variants

EC Number Protein Variants Comment Organism
6.3.3.6 E380A kcat/Km is 74.3fold lower compared to wild-type value Pectobacterium carotovorum
6.3.3.6 E380D 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 Pectobacterium carotovorum
6.3.3.6 E380Q 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 Pectobacterium carotovorum
6.3.3.6 Y345A 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 Pectobacterium carotovorum
6.3.3.6 Y345A/E380A kcat/Km is 87fold lower compared to wild-type value Pectobacterium carotovorum
6.3.3.6 Y345F 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 Pectobacterium carotovorum
6.3.3.6 Y345F/E380D kcat/Km is 87fold lower compared to wild-type value Pectobacterium carotovorum
6.3.3.6 Y345F/E380Q kcat/Km is 95fold lower compared to wild-type value Pectobacterium carotovorum

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
6.3.3.6 0.075
-
 (2S,5S)-5-carboxymethylproline pH 8.0, 25°C, mutant enzyme E380Q Pectobacterium carotovorum
6.3.3.6 0.27
-
 (2S,5S)-5-carboxymethylproline pH 8.0, 25°C, mutant enzyme Y345F Pectobacterium carotovorum
6.3.3.6 0.35
-
 (2S,5S)-5-carboxymethylproline pH 8.0, 25°C, wild-type enzyme Pectobacterium carotovorum
6.3.3.6 0.36
-
 (2S,5S)-5-carboxymethylproline pH 8.0, 25°C, mutant enzyme E380D Pectobacterium carotovorum
6.3.3.6 0.4
-
 (2S,5S)-5-carboxymethylproline pH 8.0, 25°C, mutant enzyme Y345F/E380A Pectobacterium carotovorum
6.3.3.6 0.49
-
 (2S,5S)-5-carboxymethylproline pH 8.0, 25°C, mutant enzyme E380A Pectobacterium carotovorum
6.3.3.6 0.49
-
 (2S,5S)-5-carboxymethylproline pH 8.0, 25°C, mutant enzyme Y345F/E380D Pectobacterium carotovorum
6.3.3.6 0.9
-
 (2S,5S)-5-carboxymethylproline pH 8.0, 25°C, mutant enzyme Y345F/E380Q Pectobacterium carotovorum
6.3.3.6 1.7
-
 (2S,5S)-5-carboxymethylproline pH 8.0, 25°C, mutant enzyme Y345A Pectobacterium carotovorum

Organism

EC Number Organism UniProt Comment Textmining
6.3.3.6 Pectobacterium carotovorum
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
6.3.3.6 ATP + (2S,5S)-5-carboxymethylproline catalytic Tyr-Glu dyad is demonstrated by site-directed mutagenesis and kinetic experiments that compare the wild-type enzymes to their respective mutant proteins using pH–rate profiles, 32P-incorporation experiments, solvent isotope effects, proton inventory, and viscosity variation Pectobacterium carotovorum AMP + diphosphate + (3S,5S)-carbapenam 3-carboxylate
-
 ?

Synonyms

EC Number Synonyms Comment Organism
6.3.3.6 CPS
-
 Pectobacterium carotovorum

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
6.3.3.6 25
-
 assay at Pectobacterium carotovorum

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
6.3.3.6 0.0051
-
 (2S,5S)-5-carboxymethylproline pH 8.0, 25°C, mutant enzyme Y345F/E380A Pectobacterium carotovorum
6.3.3.6 0.0059
-
 (2S,5S)-5-carboxymethylproline pH 8.0, 25°C, mutant enzyme Y345F/E380D Pectobacterium carotovorum
6.3.3.6 0.0067
-
 (2S,5S)-5-carboxymethylproline pH 8.0, 25°C, mutant enzyme E380A Pectobacterium carotovorum
6.3.3.6 0.011
-
 (2S,5S)-5-carboxymethylproline pH 8.0, 25°C, mutant enzyme Y345A Pectobacterium carotovorum
6.3.3.6 0.011
-
 (2S,5S)-5-carboxymethylproline pH 8.0, 25°C, mutant enzyme Y345F/E380Q Pectobacterium carotovorum
6.3.3.6 0.02
-
 (2S,5S)-5-carboxymethylproline pH 8.0, 25°C, mutant enzyme E380Q Pectobacterium carotovorum
6.3.3.6 0.17
-
 (2S,5S)-5-carboxymethylproline pH 8.0, 25°C, mutant enzyme Y345F Pectobacterium carotovorum
6.3.3.6 0.26
-
 (2S,5S)-5-carboxymethylproline pH 8.0, 25°C, mutant enzyme E380D Pectobacterium carotovorum
6.3.3.6 0.36
-
 (2S,5S)-5-carboxymethylproline pH 8.0, 25°C, wild-type enzyme Pectobacterium carotovorum

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
6.3.3.6 0.0063
-
 (2S,5S)-5-carboxymethylproline pH 8.0, 25°C, mutant enzyme Y345A Pectobacterium carotovorum
6.3.3.6 0.011
-
 (2S,5S)-5-carboxymethylproline pH 8.0, 25°C, mutant enzyme Y345F/E380Q Pectobacterium carotovorum
6.3.3.6 0.012
-
 (2S,5S)-5-carboxymethylproline pH 8.0, 25°C, mutant enzyme Y345F/E380A Pectobacterium carotovorum
6.3.3.6 0.012
-
 (2S,5S)-5-carboxymethylproline pH 8.0, 25°C, mutant enzyme Y345F/E380D Pectobacterium carotovorum
6.3.3.6 0.014
-
 (2S,5S)-5-carboxymethylproline pH 8.0, 25°C, mutant enzyme E380A Pectobacterium carotovorum
6.3.3.6 0.27
-
 (2S,5S)-5-carboxymethylproline pH 8.0, 25°C, mutant enzyme E380Q Pectobacterium carotovorum
6.3.3.6 0.63
-
 (2S,5S)-5-carboxymethylproline pH 8.0, 25°C, mutant enzyme Y345F Pectobacterium carotovorum
6.3.3.6 0.72
-
 (2S,5S)-5-carboxymethylproline pH 8.0, 25°C, mutant enzyme E380D Pectobacterium carotovorum
6.3.3.6 1.04
-
 (2S,5S)-5-carboxymethylproline pH 8.0, 25°C, wild-type enzyme Pectobacterium carotovorum