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Literature summary extracted from

  • Goto, M.; Muramatsu, H.; Mihara, H.; Kurihara, T.; Esaki, N.; Omi, R.; Miyahara, I.; Hirotsu, K.
    Crystal structures of DELTA1-piperideine-2-carboxylate/DELTA1-pyrroline-2-carboxylate reductase belonging to a new family of NAD(P)H-dependent oxidoreductases: conformational change, substrate recognition, and stereochemistry of the reaction (2005), J. Biol. Chem., 280, 40875-40884.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.5.1.1 unliganded enzyme, in complex with NADPH, and in complex with NADPH and pyrrole-2-carboxylate Pseudomonas syringae
1.5.1.21 unliganded form, in complex with NADPH, and with NADPH and pyrrole-2-carboxylate. subunit consists of domain I, NADPH-binding domain II, and domain III. Identification of catalytic Asp-Ser-His triad Pseudomonas syringae

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.5.1.21 2-picolinate
-
 Pseudomonas syringae
1.5.1.21 pyrrole-2-carboxylate
-
 Pseudomonas syringae

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.5.1.21 36000
-
 2 * 36000, SDS-PAGE, crystallization data Pseudomonas syringae

Organism

EC Number Organism UniProt Comment Textmining
1.5.1.1 Pseudomonas syringae Q4U331
-
-
1.5.1.21 Pseudomonas syringae Q4U331
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
1.5.1.1 L-proline + NAD(P)+ = 1-pyrroline-2-carboxylate + NAD(P)H + H+ Mobile domains I and II of protein change their conformations to produce the catalytic form. Preference for NADPH over NADH is explained by the cofactor binding site architecture Pseudomonas syringae
a

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.5.1.21 140
-
 substrate pyruvate, 30°C, pH 10.0 Pseudomonas syringae
1.5.1.21 150
-
 substrate DELTA1-piperideine-2-carboxylate, 30°C, pH 10.0 Pseudomonas syringae
1.5.1.21 390
-
 substrate DELTA1-pyrroline-2-carboxylate, 30°C, pH 10.0 Pseudomonas syringae

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.5.1.21 alpha-ketobutanoate + methylamine + NADPH 10% of the rate with pyruvate Pseudomonas syringae N-methyl-2-aminobutanoate + NADP+ + H2O
-
 ?
1.5.1.21 alpha-ketohexanoate + methylamine + NADPH 23% of the rate with pyruvate Pseudomonas syringae N-methyl-2-aminohexanoate + NADP+ + H2O
-
 ?
1.5.1.21 DELTA1-piperideine-2-carboxylate + NADPH
-
 Pseudomonas syringae L-pipecolate + NADP+
-
 ?
1.5.1.21 DELTA1-pyrroline-2-carboxylate + NADPH
-
 Pseudomonas syringae L-proline + NADP+
-
 ?
1.5.1.21 fluoropyruvate + methylamine + NADPH 14% of the rate with pyruvate Pseudomonas syringae N-methylfluoroalanine + NADP+ + H2O
-
 ?
1.5.1.21 additional information no substrate: alpha-ketovalerate, ammonia Pseudomonas syringae ?
-
 ?
1.5.1.21 phenylpyruvate + methylamine + NADPH 6.3% of the rate with pyruvate Pseudomonas syringae N-methylphenylalanine + NADP+ + H2O
-
 ?
1.5.1.21 pyruvate + methylamine
-
 Pseudomonas syringae N-methylalanine
-
 ?

Subunits

EC Number Subunits Comment Organism
1.5.1.1 dimer crystallization data Pseudomonas syringae
1.5.1.21 dimer 2 * 36000, SDS-PAGE, crystallization data Pseudomonas syringae

Synonyms

EC Number Synonyms Comment Organism
1.5.1.21 DpkA
-
 Pseudomonas syringae

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.5.1.21 30 45
-
 Pseudomonas syringae

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
1.5.1.21
-
 35 stable for at least 30 min, pH 7.0 Pseudomonas syringae

Cofactor

EC Number Cofactor Comment Organism Structure
1.5.1.1 NADP+ preference for NADPH over NADH Pseudomonas syringae
1.5.1.1 NADPH preference for NADPH over NADH Pseudomonas syringae
1.5.1.21 NADH specific activity with NADPH is 88fold higher than with NADH. Preferrence of NADPH over NADH is explained by cofactor binding site architecture Pseudomonas syringae
1.5.1.21 NADPH specific activity with NADPH is 88fold higher than with NADH. Preferrence of NADPH over NADH is explained by cofactor binding site architecture Pseudomonas syringae