EC number:1.6.1.3
Enzyme
Download| EC Tree |
| 1. Oxidoreductases |
| 1.6 Acting on NADH or NADPH |
| 1.6.1 With NAD+ or NADP+ as acceptor |
| ID: | 1.6.1.3 |
|---|---|
| Description: | NAD(P)(+) transhydrogenase. |
| Alternative Name: |
Pyridine nucleotide transhydrogenase. Pyridine nucleotide transferase. Nicotinamide nucleotide transhydrogenase. NADPH-NAD(+) transhydrogenase. NADPH-NAD(+) oxidoreductase. NADH-NADP(+)-transhydrogenase. NADH transhydrogenase. NAD(+) transhydrogenase. |
3D structure
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External Links
| UniProtKB Enzyme Link: | UniProtKB 1.6.1.3 |
| BRENDA Enzyme Link: | BRENDA 1.6.1.3 |
| KEGG Enzyme Link: | KEGG1.6.1.3 |
| BioCyc Enzyme Link: | BioCyc 1.6.1.3 |
| ExPASy Enzyme Link: | ExPASy1.6.1.3 |
| EC2PDB Enzyme Link: | EC2PDB 1.6.1.3 |
| ExplorEnz Enzyme Link: | ExplorEnz 1.6.1.3 |
| PRIAM enzyme-specific profiles Link: | PRIAM 1.6.1.3 |
| IntEnz Enzyme Link: | IntEnz 1.6.1.3 |
| MEDLINE Enzyme Link: | MEDLINE 1.6.1.3 |
| RHEA:11692 | NAD(+) + NADPH = NADH + NADP(+) |
| RULE(radius=1) | [*:1]-[O;H0;+0:2]-[P;H0;+0:3](=[*:4])(-[*:5])-[*:6].[*:7]-[OH;+0:8]>>[*:1]-[OH;+0:2].[*:4]=[P;H0;+0:3](-[*:5])(-[*:6])-[O;H0;+0:8]-[*:7] |
| Reaction |  |
| Core-to-Core | No scaffolds atoms were exchanged as a result of the reaction |
References
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| Structures of the dI2dIII1 complex of proton-translocating transhydrogenase with bound, inactive analogues of NADH and NADPH reveal active site geometries. | Bhakta T, Whitehead SJ, Snaith JS, Dafforn TR, Wilkie J, Rajesh S, White SA, Jackson JB | 2007 Mar 20 | 17323922 |
| The role of invariant amino acid residues at the hydride transfer site of proton-translocating transhydrogenase. | Brondijk TH, van Boxel GI, Mather OC, Quirk PG, White SA, Jackson JB | 2006 May 12 | 16533815 |
| Differential inhibition of six copper amine oxidases by a family of 4-(aryloxy)-2-butynamines: evidence for a new mode of inactivation. | O'Connell KM, Langley DB, Shepard EM, Duff AP, Jeon HB, Sun G, Freeman HC, Guss JM, Sayre LM, Dooley DM | 2004 Aug 31 | 15323556 |
| Interactions between transhydrogenase and thio-nicotinamide Analogues of NAD(H) and NADP(H) underline the importance of nucleotide conformational changes in coupling to proton translocation. | Singh A, Venning JD, Quirk PG, van Boxel GI, Rodrigues DJ, White SA, Jackson JB | 2003 Aug 29 | 12791694 |
| Glutamine 132 in the NAD(H)-binding component of proton-translocating transhydrogenase tethers the nucleotides before hydride transfer. | van Boxel GI, Quirk PG, Cotton NP, White SA, Jackson JB | 2003 Feb 11 | 12564924 |
| Link between the membrane-bound pyridine nucleotide transhydrogenase and glutathione-dependent processes in Rhodobacter sphaeroides. | Hickman JW, Barber RD, Skaar EP, Donohue TJ | 2002 Jan | 11751816 |
| A change in ionization of the NADP(H)-binding component (dIII) of proton-translocating transhydrogenase regulates both hydride transfer and nucleotide release. | Rodrigues DJ, Venning JD, Quirk PG, Jackson JB | 2001 Mar | 11231296 |
| X-ray structure of domain I of the proton-pumping membrane protein transhydrogenase from Escherichia coli. | Johansson T, Oswald C, Pedersen A, Törnroth S, Okvist M, Karlsson BG, Rydström J, Krengel U | 2005 Sep 16 | 16083909 |