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Literature summary extracted from

  • Moxley, M.A.; Sanyal, N.; Krishnan, N.; Tanner, J.J.; Becker, D.F.
    Evidence for hysteretic substrate channeling in the proline dehydrogenase and delta1-pyrroline-5-carboxylate dehydrogenase coupled reaction of proline utilization A (PutA) (2014), J. Biol. Chem., 289, 3639-3651.
    View publication on PubMedView publication on EuropePMC

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.2.1.88 0.022
-
 NAD+ pH 7.5, 21°C Escherichia coli
1.2.1.88 0.0235
-
 NAD+ overall reaction of bifunctional enzyme, pH 7.5, 21°C Escherichia coli
1.2.1.88 2
-
 1-pyrroline-5-carboxylate pH 7.5, 21°C Escherichia coli
1.5.5.2 0.0235
-
 NAD+ overall reaction of bifunctional enzyme, pH 7.5, 21°C Escherichia coli
1.5.5.2 2
-
 L-proline pH 7.5, 21°C Escherichia coli
1.5.5.2 42
-
 NAD+ pH 7.5, 21°C Escherichia coli

Organism

EC Number Organism UniProt Comment Textmining
1.2.1.88 Escherichia coli P09546 bifunctional proline dehydrogenase and delta1-pyrroline-5-carboxylate dehydrogenase, reactions of EC 1.5.5.2 and 1.2.1.88, respectively
-
1.5.5.2 Escherichia coli P09546 bifunctional proline dehydrogenase and delta1-pyrroline-5-carboxylate dehydrogenase, reactions of EC 1.5.5.2 and EC 1.2.1.88, respectively
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.2.1.88 1-pyrroline-5-carboxylate + NAD+ + H2O
-
 Escherichia coli L-glutamate + NADH + H+
-
 ?
1.2.1.88 L-glutamate 5-semialdehyde + NAD+ + H2O
-
 Escherichia coli L-glutamate + NADH + H+ two-electron oxidation in which a hydride is transferred toNAD+, producing NADH and glutamate ?
1.2.1.88 additional information kinetic model for the overall PRODH-P5CDH reaction of bifunctional PutA enzyme. The intermediate is not released into the bulk medium, but the mechanism follows substrate channeling. The rate of NADH formation is 20fold slower than the steady-state turnover number for the overall reaction, The limiting rate constant observed for NADH formation in the first turnover increases by almost 40fold after multiple turnovers, achieving half of the steady-state value after 15 turnovers Escherichia coli ?
-
 ?
1.5.5.2 L-proline + NAD+ + H2O
-
 Escherichia coli (S)-1-pyrroline-5-carboxylate + NADH
-
 ?
1.5.5.2 additional information kinetic model for the overall PRODH-P5CDH reaction of bifunctional PutA enzyme. The intermediate is not released into the bulk medium, but the mechanism follows substrate channeling. The rate of NADH formation is 20fold slower than the steady-state turnover number for the overall reaction, The limiting rate constant observed for NADH formation in the first turnover increases by almost 40fold after multiple turnovers, achieving half of the steady-state value after 15 turnovers Escherichia coli ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.2.1.88 PutA
-
 Escherichia coli
1.5.5.2 PutA
-
 Escherichia coli

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.2.1.88 5.16
-
 1-pyrroline-5-carboxylate pH 7.5, 21°C Escherichia coli
1.5.5.2 5.2
-
 L-proline pH 7.5, 21°C Escherichia coli

Cofactor

EC Number Cofactor Comment Organism Structure
1.2.1.88 NAD+
-
 Escherichia coli

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
1.2.1.88 31
-
 NAD+ overall reaction of bifunctional enzyme, pH 7.5, 21°C Escherichia coli
1.2.1.88 235
-
 NAD+ pH 7.5, 21°C Escherichia coli
1.5.5.2 0.124
-
 L-proline pH 7.5, 21°C Escherichia coli
1.5.5.2 31
-
 NAD+ overall reaction of bifunctional enzyme, pH 7.5, 21°C Escherichia coli
1.5.5.2 235
-
 NAD+ pH 7.5, 21°C Escherichia coli