1.5.5.2 hydroxy-L-proline + acceptor + H2O 3%5 the rate of L-proline Escherichia coli ? - ? 259418 1.5.5.2 L-proline + 2,6-dichlorophenolindophenol + H2O - Thermococcus profundus (S)-1-pyrroline-5-carboxylate + reduced 2,6-dichlorophenolindophenol - ? 377069 1.5.5.2 L-proline + 2,6-dichlorophenolindophenol + H2O + phenazine methosulfate as mediator Escherichia coli (S)-1-pyrroline-5-carboxylate + reduced 2,6-dichlorophenolindophenol - ? 377069 1.5.5.2 L-proline + 2,6-dichlorophenolindophenol + H2O - Escherichia coli DELTA1-pyrroline-5-carboxylate + reduced 2,6-dichlorophenolindophenol - ? 426585 1.5.5.2 L-proline + 2,6-dichlorophenolindophenol + H2O - Mycobacterium tuberculosis DELTA1-pyrroline-5-carboxylate + reduced 2,6-dichlorophenolindophenol - ? 426585 1.5.5.2 L-proline + 2,6-dichlorphenol-indophenol - Arabidopsis thaliana (S)-1-pyrroline-5-carboxylate + reduced 2,6-dichlorphenol-indophenol - ? 441544 1.5.5.2 L-proline + 2,6-dichlorphenol-indophenol - Thermococcus profundus (S)-1-pyrroline-5-carboxylate + reduced 2,6-dichlorphenol-indophenol - ? 441544 1.5.5.2 L-proline + 2,6-dichlorphenol-indophenol - Thermus thermophilus (S)-1-pyrroline-5-carboxylate + reduced 2,6-dichlorphenol-indophenol - ? 441544 1.5.5.2 L-proline + 2,6-dichlorphenol-indophenol - Pyrococcus horikoshii (S)-1-pyrroline-5-carboxylate + reduced 2,6-dichlorphenol-indophenol - ? 441544 1.5.5.2 L-proline + 2,6-dichlorphenol-indophenol - Pyrococcus furiosus (S)-1-pyrroline-5-carboxylate + reduced 2,6-dichlorphenol-indophenol - ? 441544 1.5.5.2 L-proline + 2,6-dichlorphenol-indophenol - Thermococcus kodakarensis (S)-1-pyrroline-5-carboxylate + reduced 2,6-dichlorphenol-indophenol - ? 441544 1.5.5.2 L-proline + 2,6-dichlorphenol-indophenol - Trypanosoma cruzi (S)-1-pyrroline-5-carboxylate + reduced 2,6-dichlorphenol-indophenol - ? 441544 1.5.5.2 L-proline + 2,6-dichlorphenol-indophenol - Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039 (S)-1-pyrroline-5-carboxylate + reduced 2,6-dichlorphenol-indophenol - ? 441544 1.5.5.2 L-proline + 2,6-dichlorphenol-indophenol - Thermococcus kodakarensis KOD1 JCM12380 (S)-1-pyrroline-5-carboxylate + reduced 2,6-dichlorphenol-indophenol - ? 441544 1.5.5.2 L-proline + 2,6-dichlorphenol-indophenol - Trypanosoma cruzi CL Brener (S)-1-pyrroline-5-carboxylate + reduced 2,6-dichlorphenol-indophenol - ? 441544 1.5.5.2 L-proline + 2,6-dichlorphenol-indophenol - Thermococcus profundus DSM 9503 (S)-1-pyrroline-5-carboxylate + reduced 2,6-dichlorphenol-indophenol - ? 441544 1.5.5.2 L-proline + 2,6-dichlorphenol-indophenol - Pyrococcus horikoshii OT-3 (S)-1-pyrroline-5-carboxylate + reduced 2,6-dichlorphenol-indophenol - ? 441544 1.5.5.2 L-proline + a quinone - Thermus thermophilus (S)-1-pyrroline-5-carboxylate + a quinol - ? 440303 1.5.5.2 L-proline + a quinone the reverse reaction is catalyzed by pyrroline-5-carboxylate reductase, EC 1.5.1.2 Thermus thermophilus (S)-1-pyrroline-5-carboxylate + a quinol - ir 440303 1.5.5.2 L-proline + a quinone the reverse reaction is catalyzed by pyrroline-5-carboxylate reductase, EC 1.5.1.2 Trypanosoma cruzi (S)-1-pyrroline-5-carboxylate + a quinol - ir 440303 1.5.5.2 L-proline + a quinone a FAD-dependent reaction Thermus thermophilus (S)-1-pyrroline-5-carboxylate + a quinol - ? 440303 1.5.5.2 L-proline + a quinone - Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039 (S)-1-pyrroline-5-carboxylate + a quinol - ? 440303 1.5.5.2 L-proline + a quinone a FAD-dependent reaction Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039 (S)-1-pyrroline-5-carboxylate + a quinol - ? 440303 1.5.5.2 L-proline + a quinone the reverse reaction is catalyzed by pyrroline-5-carboxylate reductase, EC 1.5.1.2 Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039 (S)-1-pyrroline-5-carboxylate + a quinol - ir 440303 1.5.5.2 L-proline + a quinone the reverse reaction is catalyzed by pyrroline-5-carboxylate reductase, EC 1.5.1.2 Trypanosoma cruzi CL Brener (S)-1-pyrroline-5-carboxylate + a quinol - ir 440303 1.5.5.2 L-proline + acceptor - Pyrococcus horikoshii (S)-1-pyrroline-5-carboxylate + reduced acceptor - ? 421996 1.5.5.2 L-proline + acceptor the bifunctional enzyme catalyzes the oxidation of proline in two steps. (S)-1-Pyrroline-5-carboxylate, the product of the first reaction is in spontaneous equilibrium with its tautomer L-glutamate gamma-semialdehyde: (1) L-proline + acceptor = (S)-1-pyrroline-5-carboxylate + reduced acceptor, (2) L-glutamate 5-semialdehyde + NAD+ + H2O = L-glutamate + NADH + H+ Escherichia coli (S)-1-pyrroline-5-carboxylate + reduced acceptor - ? 421996 1.5.5.2 L-proline + acceptor + H2O - Escherichia coli (S)-1-pyrroline-5-carboxylate + reduced acceptor - ? 259417 1.5.5.2 L-proline + acceptor + H2O - Thermococcus profundus (S)-1-pyrroline-5-carboxylate + reduced acceptor - ? 259417 1.5.5.2 L-proline + acceptor + H2O enzyme exists in soluble and in membrane associated forms differing in catalytic properties Escherichia coli (S)-1-pyrroline-5-carboxylate + reduced acceptor - ? 259417 1.5.5.2 L-proline + acceptor + H2O acceptors: 2,6-dichlorophenolindophenol, phenazine methosulfate, ferricyanide, menadione, cytochrome c Escherichia coli (S)-1-pyrroline-5-carboxylate + reduced acceptor - ? 259417 1.5.5.2 L-proline + acceptor + H2O PutA flavoprotein plays multiple roles in proline catabolism by functioning as a membrane-associated bi-functional enzyme and a transcriptional repressor of proline utilization genes Escherichia coli (S)-1-pyrroline-5-carboxylate + reduced acceptor - ? 259417 1.5.5.2 L-proline + acceptor + H2O the enzyme catalyzes the first step of proline catabolism Escherichia coli (S)-1-pyrroline-5-carboxylate + reduced acceptor - ? 259417 1.5.5.2 L-proline + cytochrome c the reverse reaction is catalyzed by pyrroline-5-carboxylate reductase, EC 1.5.1.2 Trypanosoma cruzi (S)-1-pyrroline-5-carboxylate + reduced cytochrome c - ir 441546 1.5.5.2 L-proline + cytochrome c the reverse reaction is catalyzed by pyrroline-5-carboxylate reductase, EC 1.5.1.2 Trypanosoma cruzi CL Brener (S)-1-pyrroline-5-carboxylate + reduced cytochrome c - ir 441546 1.5.5.2 L-proline + FAD + H2O - Escherichia coli (S)-1-pyrroline-5-carboxylate + FADH2 - ? 389060 1.5.5.2 L-proline + ferricyanide + H2O - Thermococcus profundus (S)-1-pyrroline-5-carboxylate + ferrocyanide - ? 377071 1.5.5.2 L-proline + NAD+ NADP+ is a poor electron acceptor Trypanosoma cruzi (S)-1-pyrroline-5-carboxylate + NADH - ? 441548 1.5.5.2 L-proline + NAD+ NADP+ is a poor electron acceptor Trypanosoma cruzi CL Brener (S)-1-pyrroline-5-carboxylate + NADH - ? 441548 1.5.5.2 L-proline + NAD+ + H2O - Escherichia coli (S)-1-pyrroline-5-carboxylate + NADH - ? 439688 1.5.5.2 L-proline + oxidized dichlorophenolindophenol - Escherichia coli 1-pyrroline-5-carboxylate + reduced dichlorophenolindophenol - ? 405644 1.5.5.2 L-proline + oxidized phenazine methosulfate - Arabidopsis thaliana (S)-1-pyrroline-5-carboxylate + reduced phenazine methosulfate - ? 440304 1.5.5.2 L-thiazolidine-4-carboxylate + acceptor + H2O - Escherichia coli N-formylcysteine + reduced acceptor - ? 259420 1.5.5.2 additional information no substrate: D-proline, other L-amino acids, L-azetidine-2-carboxylate, succinate Escherichia coli ? - ? 89 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 ? - ? 89 1.5.5.2 additional information no activity with D-proline, L-hydroxyproline, pyrrolidone-5-carboxylate, sarcosine, and glycine Thermococcus profundus ? - ? 89 1.5.5.2 additional information no activity with D-proline, L-hydroxyproline, pyrrolidone-5-carboxylate, sarcosine, and glycine Pyrococcus horikoshii ? - ? 89 1.5.5.2 additional information no activity with D-proline, L-hydroxyproline, pyrrolidone-5-carboxylate, sarcosine, and glycine Pyrococcus furiosus ? - ? 89 1.5.5.2 additional information no activity with D-proline, L-hydroxyproline, pyrrolidone-5-carboxylate, sarcosine, and glycine Thermococcus kodakarensis ? - ? 89 1.5.5.2 additional information poor activity with D-proline, hydroxyproline, L-pipecolic acid, nicotinic acid, and thiazolidine-4-carboxylic acid Trypanosoma cruzi ? - ? 89 1.5.5.2 additional information the enzyme is assayed with L-proline as substrate and 2-(p-iodophenyl)-3-(p-nitrophenyl)-5-phenyltetrazolium chloride (INT) as a terminal electron acceptor and phenazine methosulfate (PMS) as a mediator electron carrier Pseudomonas putida ? - ? 89 1.5.5.2 additional information no activity with D-proline, L-hydroxyproline, pyrrolidone-5-carboxylate, sarcosine, and glycine Thermococcus kodakarensis KOD1 JCM12380 ? - ? 89 1.5.5.2 additional information poor activity with D-proline, hydroxyproline, L-pipecolic acid, nicotinic acid, and thiazolidine-4-carboxylic acid Trypanosoma cruzi CL Brener ? - ? 89 1.5.5.2 additional information no activity with D-proline, L-hydroxyproline, pyrrolidone-5-carboxylate, sarcosine, and glycine Thermococcus profundus DSM 9503 ? - ? 89 1.5.5.2 additional information the enzyme is assayed with L-proline as substrate and 2-(p-iodophenyl)-3-(p-nitrophenyl)-5-phenyltetrazolium chloride (INT) as a terminal electron acceptor and phenazine methosulfate (PMS) as a mediator electron carrier Pseudomonas putida POS-F84 ? - ? 89 1.5.5.2 additional information no activity with D-proline, L-hydroxyproline, pyrrolidone-5-carboxylate, sarcosine, and glycine Pyrococcus horikoshii OT-3 ? - ? 89 1.5.5.2 trans-4-hydroxy-L-proline + oxidized dichlorophenolindophenol - Escherichia coli ? - ? 406792