EzCatDB: M00162

DB codeM00162
CATH domainDomain 1-.-.-.-
Domain 2-.-.-.-
Domain 3-.-.-.-
Domain 43.40.50.1220Catalytic domain
E.C.1.6.1.2
CSA1djl

CATH domainRelated DB codes (homologues)
3.40.50.1220M00161,T00237,T00230

Enzyme Name
Swiss-protKEGG

P11024Q13423
Protein nameNAD(P) transhydrogenase, mitochondrialNAD(P) transhydrogenase, mitochondrialNAD(P)+ transhydrogenase (AB-specific)
pyridine nucleotide transhydrogenase
transhydrogenase
NAD(P)+ transhydrogenase
nicotinamide adenine dinucleotide (phosphate) transhydrogenase
NAD+ transhydrogenase
NADH transhydrogenase
nicotinamide nucleotide transhydrogenase
NADPH-NAD+ transhydrogenase
pyridine nucleotide transferase
NADPH-NAD+ oxidoreductase
NADH-NADP+-transhydrogenase
NADPH:NAD+ transhydrogenase
H+-Thase
energy-linked transhydrogenase
NAD(P)+ transhydrogenase (AB-specific)
SynonymsEC 1.6.1.2
Nicotinamide nucleotide transhydrogenase
Pyridine nucleotide transhydrogenase
EC 1.6.1.2
Nicotinamide nucleotide transhydrogenase
Pyridine nucleotide transhydrogenase

KEGG pathways
MAP codePathways
MAP00760Nicotinate and nicotinamide metabolism

Swiss-prot:Accession NumberP11024Q13423
Entry nameNNTM_BOVINNNTM_HUMAN
ActivityNADPH + NAD(+) = NADP(+) + NADH.NADPH + NAD(+) = NADP(+) + NADH.
SubunitHomodimer.Homodimer (By similarity).
Subcellular locationMitochondrion inner membrane, Multi-pass membrane protein, Matrix side (Potential).Mitochondrion inner membrane, Multi-pass membrane protein, Matrix side (Potential).
Cofactor



SubstratesProducts
KEGG-idC00005C00003C00006C00004
CompoundNADPHNAD+NADP+NADH
Typeamide group,amine group,nucleotideamide group,amine group,nucleotideamide group,amine group,nucleotideamide group,amine group,nucleotide
1d4oAUnboundUnboundBound:NAPUnbound
1djlAUnboundUnboundBound:NAPUnbound
1djlBUnboundUnboundBound:NAPUnbound
1pt9AUnboundUnboundAnalogue:TAPUnbound
1pt9BUnboundUnboundAnalogue:TAPUnbound
1u31AUnboundUnboundBound:NAPUnbound
1u31BUnboundUnboundBound:NAPUnbound

Active-site residues
resource
literature [7]
pdbCatalytic residues
1d4oATYR  31;ARG  66;TYR  147
1djlATYR 890;ARG 925;TYR 1006
1djlBTYR 890;ARG 925;TYR 1006
1pt9ATYR  54;ARG  89;TYR  170
1pt9BTYR  54;ARG  89;TYR  170
1u31ATYR  54;ARG  89;TYR  170
1u31BTYR  54;ARG  89;TYR  170

References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[8]p.8-9
[10]

[11]


references
[1]
PubMed ID2361137
JournalBiochemistry
Year1990
Volume29
Pages4136-43
AuthorsYamaguchi M, Wakabayashi S, Hatefi Y
TitleMitochondrial energy-linked nicotinamide nucleotide transhydrogenase: effect of substrates on the sensitivity of the enzyme to trypsin and identification of tryptic cleavage sites.
[2]
CommentsTOPOLOGY.
Medline ID91170247
PubMed ID2005110
JournalJ Biol Chem
Year1991
Volume266
Pages5728-35
AuthorsYamaguchi M, Hatefi Y
TitleMitochondrial energy-linked nicotinamide nucleotide transhydrogenase. Membrane topography of the bovine enzyme.
Related Swiss-protP11024
[3]
PubMed ID10514549
JournalBiochim Biophys Acta
Year1999
Volume1413
Pages81-91
AuthorsPeake SJ, Venning JD, Cotton NP, Jackson JB
TitleEvidence for the stabilization of NADPH relative to NADP(+) on the dIII components of proton-translocating transhydrogenases from Homo sapiens and from Rhodospirillum rubrum by measurement of tryptophan fluorescence.
[4]
PubMed ID10216162
JournalBiochim Biophys Acta
Year1999
Volume1411
Pages159-69
AuthorsPeake SJ, Venning JD, Jackson JB
TitleA catalytically active complex formed from the recombinant dI protein of Rhodospirillum rubrum transhydrogenase, and the recombinant dIII protein of the human enzyme.
[5]
PubMed ID10587945
JournalMicrob Comp Genomics
Year1999
Volume4
Pages173-86
AuthorsStudley WK, Yamaguchi M, Hatefi Y, Saier MH Jr
TitlePhylogenetic analyses of proton-translocating transhydrogenases.
[6]
CommentsX-RAY CRYSTALLOGRAPHY (1.2 ANGSTROMS) OF 903-1086.
Medline ID20051009
PubMed ID10581554
JournalNat Struct Biol
Year1999
Volume6
Pages1126-31
AuthorsPrasad GS, Sridhar V, Yamaguchi M, Hatefi Y, Stout CD
TitleCrystal structure of transhydrogenase domain III at 1.2 A resolution.
Related PDB1d4o
Related Swiss-protP11024
[7]
PubMed ID10611473
JournalFEBS Lett
Year1999
Volume464
Pages1-8
AuthorsJackson JB, Peake SJ, White SA
TitleStructure and mechanism of proton-translocating transhydrogenase.
[8]
CommentsX-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 880-1086.
Medline ID20139687
PubMed ID10673423
JournalStructure Fold Des
Year2000
Volume8
Pages1-12
AuthorsWhite SA, Peake SJ, McSweeney S, Leonard G, Cotton NP, Jackson JB
TitleThe high-resolution structure of the NADP(H)-binding component (dIII) of proton-translocating transhydrogenase from human heart mitochondria.
Related PDB1djl
Related Swiss-protQ13423
[9]
PubMed ID11231296
JournalEur J Biochem
Year2001
Volume268
Pages1430-8
AuthorsRodrigues DJ, Venning JD, Quirk PG, Jackson JB
TitleA change in ionization of the NADP(H)-binding component (dIII) of proton-translocating transhydrogenase regulates both hydride transfer and nucleotide release.
[10]
CommentsX-ray crystallography
PubMed ID12791694
JournalJ Biol Chem
Year2003
Volume278
Pages33208-16
AuthorsSingh A, Venning JD, Quirk PG, van Boxel GI, Rodrigues DJ, White SA, Jackson JB
TitleInteractions between transhydrogenase and thio-nicotinamide Analogues of NAD(H) and NADP(H) underline the importance of nucleotide conformational changes in coupling to proton translocation.
Related PDB1pt9,1ptj
[11]
PubMed ID15323555
JournalBiochemistry
Year2004
Volume43
Pages10952-64
AuthorsMather OC, Singh A, van Boxel GI, White SA, Jackson JB
TitleActive-site conformational changes associated with hydride transfer in proton-translocating transhydrogenase.
Related PDB1u28,1u2d,1u2g,1u31

comments
This enzyme is composed of three domains, N-terminal matrix domain, membrane-intercalated domain with proton channel, and C-terminal matrix domain. Although the structures for the C-terminal domain has been solved, those of the other domains have not been determined yet. However, the N-terminal domain seems to be homologous to the alpha-1 subunit of the counterpart of bacterial enzyme (Swiss-prot;Q60164).

createdupdated
2004-12-172009-02-26
Copyright: Nozomi Nagano, JST & CBRC-AIST
Funded by PRESTO/Japan Science and Technology Corporation (JST) (December 2001 - November 2004)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2006)
Funded by Grant-in-Aid for Scientific Research (B)/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2008)
Funded by BIRD/Japan Science and Technology Corporation (JST) (September 2005 - September 2010)
Funded by BIRD/Japan Science and Technology Corporation (JST) (October 2007 - September 2010)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2011 - March 2012)

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