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Literature summary for 1.5.5.2 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
Search for more literature for 1.5.5.2

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0235
-
 NAD+ overall reaction of bifunctional enzyme, pH 7.5, 21°C Escherichia coli
2
-
 L-proline pH 7.5, 21°C Escherichia coli
42
-
 NAD+ pH 7.5, 21°C Escherichia coli

Organism

Organism UniProt Comment Textmining
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)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-proline + NAD+ + H2O
-
 Escherichia coli (S)-1-pyrroline-5-carboxylate + NADH
-
 ?
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

Synonyms Comment Organism
PutA
-
 Escherichia coli

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
5.2
-
 L-proline pH 7.5, 21°C Escherichia coli

kcat/KM [mM/s]

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