1.5.5.2: proline dehydrogenase

This is an abbreviated version!
For detailed information about proline dehydrogenase, go to the full flat file.

Word Map on EC 1.5.5.2

Reaction

L-proline
+
a quinone
=
(S)-1-pyrroline-5-carboxylate
+
a quinol

Synonyms

bifunctional dye-linked L-proline/NADH dehydrogenase complex, dye-linked L-proline dehydrogenase, FAD-dependent L-proline oxidoreductase, JcProDH, L-proline dehydrogenase, L-proline:FAD oxidoreductase, PdhB, PDHbeta, PF1246, PF1798, PH1364, PH1751, PRODH, proDH-B1, proDH-B2, PRODH/POX, ProDH1, proline dehydrogenase, proline dehydrogenase 1, proline dehydrogenase/oxidase, proline oxidase, proline/P5C dehydrogenase, prub, PutA, PutA flavoprotein, PutA proline dehydrogenase, Tc00.1047053506411.30, TcPRODH, TK0117, TK0122, TPpdhbeta, TtProDH

ECTree

     1 Oxidoreductases
         1.5 Acting on the CH-NH group of donors
             1.5.5 With a quinone or similar compound as acceptor
                1.5.5.2 proline dehydrogenase

Reference

Reference on EC 1.5.5.2 - proline dehydrogenase

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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Wood, J.M.
Membrane association of proline dehydrogenase in Escherichia coli is redox dependent
Proc. Natl. Acad. Sci. USA
84
373-377
1987
Escherichia coli
Manually annotated by BRENDA team
Graham, S.B.; Stephenson, J.T.; Wood, J.M.
Proline dehydrogenase from Escherichia coli K12. Reconstitution of a functional membrane association
J. Biol. Chem.
259
2656-2661
1984
Escherichia coli
Manually annotated by BRENDA team
Scarpulla, R.C.; Soffer, R.L.
Membrane-bound proline dehydrogenase from Escherichia coli. Solubilization, purification, and characterization
J. Biol. Chem.
253
5997-6001
1978
Escherichia coli
Manually annotated by BRENDA team
Nadaraia, S.; Lee, Y.H.; Becker, D.F.; Tanner, J.J.
Crystallization and preliminary crystallographic analysis of the proline dehydrogenase domain of the multifunctional PutA flavoprotein from Escherichia coli
Acta Crystallogr. Sect. D
57
1925-1927
2001
Escherichia coli
Manually annotated by BRENDA team
Deutch, C.E.
Oxidation of L-thiazolidine-4-carboxylate by L-proline dehydrogenase in Escherichia coli
J. Gen. Microbiol.
138
1593-1598
1992
Escherichia coli
-
Manually annotated by BRENDA team
Sakuraba, H.; Takamatsu, Y.; Satomura, T.; Kawakami, R.; Ohshima, T.
Purification, characterization, and application of a novel dye-linked L-proline dehydrogenase from a hyperthermophilic archaeon, Thermococcus profundus
Appl. Environ. Microbiol.
67
1470-1475
2001
Thermococcus profundus
Manually annotated by BRENDA team
Brown, E.D.; Wood, J.M.
Conformational change and membrane association of the PutA protein are coincident with reduction of its FAD cofactor by proline
J. Biol. Chem.
268
8972-8979
1993
Escherichia coli
Manually annotated by BRENDA team
Chaudhary, S.; Dudeja, S.S.; Sharma, H.R.; Khurana, A.L.; Malik, M.S.
Proline dehydrogenase activity of mungbean rhizobia and their proline prototrophs in relation to their efficacy in symbiotic association
Indian J. Exp. Biol.
37
1234-1240
1999
Vigna radiata
-
Manually annotated by BRENDA team
Zhang, M.; White, T.A.; Schuermann, J.P.; Baban, B.A.; Becker, D.F.; Tanner, J.J.
Structures of the Escherichia coli PutA proline dehydrogenase domain in complex with competitive inhibitors
Biochemistry
43
12539-12548
2004
Escherichia coli, Escherichia coli (P09546)
Manually annotated by BRENDA team
Baban, B.A.; Vinod, M.P.; Tanner, J.J.; Becker, D.F.
Probing a hydrogen bond pair and the FAD redox properties in the proline dehydrogenase domain of Escherichia coli PutA
Biochim. Biophys. Acta
1701
49-59
2004
Escherichia coli
Manually annotated by BRENDA team
Kawakami, R.; Sakuraba, H.; Ohshima, T.
Gene and primary structures of dye-linked L-proline dehydrogenase from the hyperthermophilic archaeon Thermococcus profundus show the presence of a novel heterotetrameric amino acid dehydrogenase complex
Extremophiles
8
99-108
2004
Thermococcus profundus (Q76M73), Thermococcus profundus (Q76M76), Thermococcus profundus
Manually annotated by BRENDA team
Lee, Y.H.; Nadaraia, S.; Gu, D.; Becker, D.F.; Tanner, J.J.
Structure of the proline dehydrogenase domain of the multifunctional PutA flavoprotein
Nat. Struct. Biol.
10
109-114
2003
Escherichia coli, Escherichia coli (P09546)
Manually annotated by BRENDA team
Zhu, W.; Becker, D.F.
Exploring the proline-dependent conformational change in the multifunctional PutA flavoprotein by tryptophan fluorescence spectroscopy
Biochemistry
44
12297-12306
2005
Escherichia coli
Manually annotated by BRENDA team
Ostrander, E.L.; Larson, J.D.; Schuermann, J.P.; Tanner, J.J.
A conserved active site tyrosine residue of proline dehydrogenase helps enforce the preference for proline over hydroxyproline as the substrate
Biochemistry
48
951-959
2009
Escherichia coli, Escherichia coli (P09546)
Manually annotated by BRENDA team
Srivastava, D.; Zhu, W.; Johnson, W.H.; Whitman, C.P.; Becker, D.F.; Tanner, J.J.
The structure of the proline utilization a proline dehydrogenase domain inactivated by N-propargylglycine provides insight into conformational changes induced by substrate binding and flavin reduction
Biochemistry
49
560-569
2010
Escherichia coli, Escherichia coli (P09546)
Manually annotated by BRENDA team
Brown, E.D.; Wood, J.M.
Redesigned purification yields a fully functional PutA protein dimer from Escherichia coli
J. Biol. Chem.
267
13086-13092
1992
Escherichia coli, Escherichia coli (P09546)
Manually annotated by BRENDA team
Moxley, M.A.; Becker, D.F.
Rapid reaction kinetics of proline dehydrogenase in the multifunctional proline utilization A protein
Biochemistry
51
511-520
2012
Escherichia coli
Manually annotated by BRENDA team
Serrano, H.; Blanchard, J.S.
Kinetic and isotopic characterization of L-proline dehydrogenase from Mycobacterium tuberculosis
Biochemistry
52
5009-5015
2013
Mycobacterium tuberculosis
Manually annotated by BRENDA team
Kawakami, R.; Satomura, T.; Sakuraba, H.; Ohshima, T.
L-proline dehydrogenases in hyperthermophilic archaea: distribution, function, structure, and application
Appl. Microbiol. Biotechnol.
93
83-93
2012
Pyrococcus horikoshii (O59088 and O59089)
Manually annotated by BRENDA team
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)
J. Biol. Chem.
289
3639-3651
2014
Escherichia coli, Escherichia coli (P09546)
Manually annotated by BRENDA team
Hancock, C.N.; Liu, W.; Alvord, W.G.; Phang, J.M.
Co-regulation of mitochondrial respiration by proline dehydrogenase/oxidase and succinate
Amino Acids
48
859-872
2016
Homo sapiens (O43272), Mus musculus (Q9WU79)
Manually annotated by BRENDA team
Wang, H.; Ao, P.; Yang, S.; Zou, Z.; Wang, S.; Gong, M.
Molecular cloning and expression analysis of the gene encoding proline dehydrogenase from Jatropha curcas L
Appl. Biochem. Biotechnol.
175
2413-2426
2015
Jatropha curcas, Jatropha curcas (V9XZ65)
Manually annotated by BRENDA team
Kawakami, R.; Noguchi, C.; Higashi, M.; Sakuraba, H.; Ohshima, T.
Comparative analysis of the catalytic components in the archaeal dye-linked L-proline dehydrogenase complexes
Appl. Microbiol. Biotechnol.
97
3419-3427
2013
Pyrococcus furiosus (Q8U022), Pyrococcus furiosus (Q8U1G2), Pyrococcus horikoshii (O59089), Pyrococcus horikoshii (O59445), Pyrococcus horikoshii OT-3 (O59089), Pyrococcus horikoshii OT-3 (O59445), Thermococcus kodakarensis (Q5JFG2), Thermococcus kodakarensis (Q5JFG7), Thermococcus kodakarensis KOD1 JCM12380 (Q5JFG7), Thermococcus profundus (Q76M73), Thermococcus profundus DSM 9503 (Q76M73)
Manually annotated by BRENDA team
Cabassa-Hourton, C.; Schertl, P.; Bordenave-Jacquemin, M.; Saadallah, K.; Guivarch, A.; Lebreton, S.; Planchais, S.; Klodmann, J.; Eubel, H.; Crilat, E.; Lefebvre-De Vos, D.; Ghelis, T.; Richard, L.; Abdelly, C.; Carol, P.; Braun, H.P.; Savoure, A.
Proteomic and functional analysis of proline dehydrogenase 1 link proline catabolism to mitochondrial electron transport in Arabidopsis thaliana
Biochem. J.
473
2623-2634
2016
Arabidopsis thaliana, Arabidopsis thaliana (P92983)
Manually annotated by BRENDA team
Huijbers, M.M.; van Berkel, W.J.
High yields of active Thermus thermophilus proline dehydrogenase are obtained using maltose-binding protein as a solubility tag
Biotechnol. J.
10
395-403
2015
Thermus thermophilus (Q72IB8), Thermus thermophilus, Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039 (Q72IB8)
Manually annotated by BRENDA team
Schertl, P.; Cabassa, C.; Saadallah, K.; Bordenave, M.; Savoure, A.; Braun, H.P.
Biochemical characterization of proline dehydrogenase in Arabidopsis mitochondria
FEBS J.
281
2794-2804
2014
Arabidopsis thaliana
Manually annotated by BRENDA team
Omidinia, E.; Mahdizadehdehosta, R.; Mohammadi, H.S.
Expression, purification and characterization of the proline dehydrogenase domain of PutA from Pseudomonas putida POS-F84
Indian J. Microbiol.
53
297-302
2013
Pseudomonas putida (I2D0K8), Pseudomonas putida, Pseudomonas putida POS-F84 (I2D0K8), Pseudomonas putida POS-F84
Manually annotated by BRENDA team
Paes, L.S.; Suarez Mantilla, B.; Zimbres, F.M.; Pral, E.M.; Diogo de Melo, P.; Tahara, E.B.; Kowaltowski, A.J.; Elias, M.C.; Silber, A.M.
Proline dehydrogenase regulates redox state and respiratory metabolism in Trypanosoma cruzi
PLoS ONE
8
e69419
2013
Trypanosoma cruzi (Q4CVA1), Trypanosoma cruzi, Trypanosoma cruzi CL Brener (Q4CVA1)
Manually annotated by BRENDA team
Huijbers, M.M.; Martinez-Julvez, M.; Westphal, A.H.; Delgado-Arciniega, E.; Medina, M.; van Berkel, W.J.
Proline dehydrogenase from Thermus thermophilus does not discriminate between FAD and FMN as cofactor
Sci. Rep.
7
43880
2017
Thermus thermophilus (Q72IB8), Thermus thermophilus, Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039 (Q72IB8)
Manually annotated by BRENDA team