EC number:1.6.1.1

Enzyme

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     1. Oxidoreductases
        1.6 Acting on NADH or NADPH
            1.6.1 With NAD+ or NADP+ as acceptor
ID:1.6.1.1
Description:NAD(P)(+) transhydrogenase (Si-specific).
Alternative Name: Pyridine nucleotide transhydrogenase.
Nicotinamide nucleotide transhydrogenase.
NAD(P)(+) transhydrogenase (B-specific).
Prosite: PDOC00073;
PDB:
PDBScop
3LAD 8056245; 8056246; 8056247; 8056245; 8056246; 8056247;
1LPF 8056242; 8056243; 8056244; 8056242; 8056243; 8056244;
1LVL 8056239; 8056240; 8056241;
1V59 8056236; 8056237; 8056238; 8056236; 8056237; 8056238;
1JEH 8056236; 8056237; 8056238; 8056236; 8056237; 8056238;
 » show all
Cath: 3.40.50.720; 3.40.50.1220;

3D structure

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PDB

References

External Links

UniProtKB Enzyme Link: UniProtKB 1.6.1.1
BRENDA Enzyme Link: BRENDA 1.6.1.1
KEGG Enzyme Link: KEGG1.6.1.1
BioCyc Enzyme Link: BioCyc 1.6.1.1
ExPASy Enzyme Link: ExPASy1.6.1.1
EC2PDB Enzyme Link: EC2PDB 1.6.1.1
ExplorEnz Enzyme Link: ExplorEnz 1.6.1.1
PRIAM enzyme-specific profiles Link: PRIAM 1.6.1.1
IntEnz Enzyme Link: IntEnz 1.6.1.1
MEDLINE Enzyme Link: MEDLINE 1.6.1.1

EC number:1.6.1.1

MSA:

1.6.1.1;
Phylogenetic Tree:

1.6.1.1;
Uniprot:
M-CSA:
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

TitleAuthorsDatePubMed 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 JB2007 Mar 2017323922
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 JB2006 May 1216533815
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 DM2004 Aug 3115323556
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 JB2003 Aug 2912791694
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 JB2003 Feb 1112564924
Link between the membrane-bound pyridine nucleotide transhydrogenase and glutathione-dependent processes in Rhodobacter sphaeroides.Hickman JW, Barber RD, Skaar EP, Donohue TJ2002 Jan11751816
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 JB2001 Mar11231296
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 U2005 Sep 1616083909