TrxB – thioredoxin reductase (NADPH)

Name
WID	TrxB
Name	thioredoxin reductase (NADPH)
Cross references	EC: 1.8.1.9, SABIO-RK: 2435, KEGG: R02016, BioCyc: THIOREDOXIN-REDUCT-NADPH-RXN, BiGG: TRDR

Classification
Type	chemical

Reaction
Stoichiometry	[c]: H + MG_124_MONOMER_ox + NADPH ⇔ MG_124_MONOMER + NADP

Catalysis
Enzyme	MG_102_DIMER [c]
Coenzymes	(1) FAD [c] (Show evidence) Value: FAD Measured: Yes References Chang A, Scheer M, Grote A, Schomburg I, Schomburg D. BRENDA, AMENDA and FRENDA the enzyme information system: new content and tools in 2009. Nucleic Acids Res 37, D588-92 (2009). WholeCell: PUB_0570, PubMed: 18984617 Value: FAD Measured: Yes Species: Escherichia coli K12 References Keseler IM, Bonavides-Martínez C, Collado-Vides J, Gama-Castro S, Gunsalus RP, Johnson DA, Krummenacker M, Nolan LM, Paley S, Paulsen IT, Peralta-Gil M, Santos-Zavaleta A, Shearer AG, Karp PD. EcoCyc: a comprehensive view of Escherichia coli biology. Nucleic Acids Res 37, D464-70 (2009). WholeCell: PUB_0006, PubMed: 18974181 Value: FAD Measured: Yes Species: Escherichia coli K-12 MG1655 Comments Binds 1 FAD per subunit. References UniProt Consortium. The Universal Protein Resource (UniProt) 2009. Nucleic Acids Res 37, D169-74 (2009). WholeCell: PUB_0096, PubMed: 18836194, URL: http://www.uniprot.org/uniprot/
Optimal pH	7.6 (dimensionless)
Optimal temperature	44.0 (C)

Energetics
Is spontaneous (pH 7.5, 25C, I = 0)	False

Kinetics
Forward kinetics	v = V_max * [MG_124_MONOMER_ox] / (K_m + [MG_124_MONOMER_ox]); K_m = 1.5 (nM), V_max = 1250.0 1/min (Show evidence) Value: Rate law: VmaxOTHIO/(Km+OTHIO); Km = 1.5 uM, Vmax = 1250 1/min (None) Measured: Yes* Species: Escherichia coli References Wittig U, Golebiewski M, Kania R, Krebs O, Mir S, Weidemann A, Anstein S, Saric J, Rojas I. In proceedings of the 3rd International workshop on Data Integration in the Life Sciences 2006. Lecture Notes in Bioinformatics 4075, 94-103 (2006). WholeCell: PUB_0100, URL: http://sabio.villa-bosch.de/

Associations
Pathways	OXIDATIVE_PHOSPHORYLATION
Process	Process_Metabolism

Comments
References	Chang A, Scheer M, Grote A, Schomburg I, Schomburg D. BRENDA, AMENDA and FRENDA the enzyme information system: new content and tools in 2009. Nucleic Acids Res 37, D588-92 (2009). WholeCell: PUB_0570, PubMed: 18984617 Keseler IM, Bonavides-Martínez C, Collado-Vides J, Gama-Castro S, Gunsalus RP, Johnson DA, Krummenacker M, Nolan LM, Paley S, Paulsen IT, Peralta-Gil M, Santos-Zavaleta A, Shearer AG, Karp PD. EcoCyc: a comprehensive view of Escherichia coli biology. Nucleic Acids Res 37, D464-70 (2009). WholeCell: PUB_0006, PubMed: 18974181 UniProt Consortium. The Universal Protein Resource (UniProt) 2009. Nucleic Acids Res 37, D169-74 (2009). WholeCell: PUB_0096, PubMed: 18836194, URL: http://www.uniprot.org/uniprot/ Wittig U, Golebiewski M, Kania R, Krebs O, Mir S, Weidemann A, Anstein S, Saric J, Rojas I. In proceedings of the 3rd International workshop on Data Integration in the Life Sciences 2006. Lecture Notes in Bioinformatics 4075, 94-103 (2006). WholeCell: PUB_0100, URL: http://sabio.villa-bosch.de/

Metadata
Created	2012-10-01 15:09:02
Last updated	2012-10-01 15:17:56