Overview for MACiE Entry M0116
EC Number: 188.8.131.52 (A member of the Oxidoreductases, Acting on NADH or NADPH, With NAD+ or NADP+ as acceptor)
Enzyme Name: NAD(P)+ transhydrogenase (AB-specific)
Biological Species: Rhodospirillum rubrum (Bacteria)
Catalytic Chain UniprotKB Accession Codes:
- Q2RSB2 - NAD(P) transhydrogenase subunit alpha part 1
- Q2RSB4 - NAD(P) transhydrogenase subunit beta
Representative PDB Code: 1hzz - THE ASYMMETRIC COMPLEX OF THE TWO NUCLEOTIDE-BINDINGCOMPONENTS (DI, DIII) OF PROTON-TRANSLOCATINGTRANSHYDROGENASE (Resolution = 2.50 Å).
Display structure information
Overall Comment: This enzyme couples the transfer of reducing equivalents (hydride-ion equivalents) between NAD(H) and NADP(H) to inward proton translocation across mitochondrial and bacterial membranes. The coupling reactions occur within the protein by long distance conformational changes of the reducing equivalents.
View similar reactions
Stepwise Description of the Reaction
|Step 1||Asp132C obtains a proton, causing a rearrangement of the active site.|
|Step 2||NAD eliminates a hydride ion, which adds to NADP.|
|Step 3||Asp132C releases its proton.|
View similar reactions (composite manual annotation)
Catalytic Residues Involved
||Location of Function
- D. J. Rodrigues et al. (2001), Eur. J. Biochem., 268, 1430-1438. A change in ionization of the NADP(H)-binding component (dIII) of proton-translocating transhydrogenase regulates both hydride transfer and nucleotide release.
- G. I. van Boxel et al. (2003), Biochemistry, 42, 1217-1226. Glutamine 132 in the NAD(H)-binding component of proton-translocating transhydrogenase tethers the nucleotides before hydride transfer.
- O. C. Mather et al. (2004), Biochemistry, 43, 10952-10964. Differential inhibition of six copper amine oxidases by a family of 4-(aryloxy)-2-butynamines: evidence for a new mode of inactivation.
- A. Singh et al. (2003), J. Biol. Chem., 278, 33208-33216. 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.
Homologue information for M0116 (1hzz)
MACiE Homologues (within the PDB)
MACiE Homologues (within UniprotKB/SwissProt)
Entries with at least one Catalytic CATH code in common (different mechanisms):
|M0255 ||alcohol dehydrogenase |
|M0092 ||UDP-glucose 6-dehydrogenase |
|M0021 ||malate dehydrogenase (oxaloacetate-decarboxylating) |
|M0227 ||GDP-L-fucose synthase |
|M0067 ||alanine dehydrogenase |
|M0110 ||D-amino-acid oxidase |
|M0237 ||pteridine reductase |
|M0142 ||ferredoxin-NADP+ reductase |
|M0090 ||adenosylhomocysteinase |
|M0240 ||histone/protein deacetylase |
|M0226 ||UDP-sulfoquinovose synthase |
|M0220 ||benzoylformate decarboxylase |
|M0228 ||dTDP-glucose 4,6-dehydratase |
|M0188 ||UDP-glucose 4-epimerase |
View a comparison of the other reactions in MACiE with the CATH domain 184.108.40.2060
View a comparison of the other reactions in MACiE with the CATH domain 220.127.116.110
Links to this entry in other databases