NAD/NADP-NADH/NADPH mitochondrial interconversion (yeast)

Feng Y, Li W, Li J, Wang J, Ge J, Xu D, Liu Y, Wu K, Zeng Q, Wu JW, Tian C, Zhou B, Yang M. Structural insight into the type-II mitochondrial NADH dehydrogenases. Nature. 2012 Nov 15;491(7424):478–82. doi: 10.1038/nature11541. PMID: 23086143.; Gossmann TI, Ziegler M, Puntervoll P, de Figueiredo LF, Schuster S, Heiland I. NAD+ biosynthesis and salvage – a phylogenetic perspective. The FEBS Journal. 2012 Apr 04;279(18):3355–63. doi: 10.1111/j.1742-4658.2012.08559.x.; Lu S, Lin S. Phosphate-responsive Signaling Pathway Is a Novel Component of NAD+ Metabolism in Saccharomyces cerevisiae. Journal of Biological Chemistry. 2011 Apr;286(16):14271–81. doi: 10.1074/jbc.m110.217885.; Miyagi H, Kawai S, Murata K. Two Sources of Mitochondrial NADPH in the Yeast Saccharomyces cerevisiae. Journal of Biological Chemistry. 2009 Mar;284(12):7553–60. doi: 10.1074/jbc.m804100200.; Koch-Nolte F, Haag F, Guse AH, Lund F, Ziegler M. Emerging Roles of NAD + and Its Metabolites in Cell SignalingA report on the NAD2008 symposium, Hamburg, Germany, 14 to 17 September 2008. Sci. Signal. 2009 Feb 10;2(57). doi: 10.1126/scisignal.257mr1.; Bieganowski P, Seidle HF, Wojcik M, Brenner C. Synthetic Lethal and Biochemical Analyses of NAD and NADH Kinases in Saccharomyces cerevisiae Establish Separation of Cellular Functions. Journal of Biological Chemistry. 2006 Aug;281(32):22439–45. doi: 10.1074/jbc.m513919200.; Strand MK, Stuart GR, Longley MJ, Graziewicz MA, Dominick OC, Copeland WC. POS5 Gene of Saccharomyces cerevisiae Encodes a Mitochondrial NADH Kinase Required for Stability of Mitochondrial DNA. Eukaryot Cell. 2003 Aug;2(4):809–20. doi: 10.1128/ec.2.4.809-820.2003.; Outten CE, Culotta VC. A novel NADH kinase is the mitochondrial source of NADPH in Saccharomyces cerevisiae. EMBO J. 2003 May 01;22(9):2015–24. PMID: 12727869; PMCID: PMC156083.; Påhlman I, Larsson C, Averét N, Bunoust O, Boubekeur S, Gustafsson L, Rigoulet M. Kinetic Regulation of the Mitochondrial Glycerol-3-phosphate Dehydrogenase by the External NADH Dehydrogenase in Saccharomyces cerevisiae. Journal of Biological Chemistry. 2002 Aug;277(31):27991–5. doi: 10.1074/jbc.m204079200.; Overkamp KM, Bakker BM, Ko¨tter P, van Tuijl A, de Vries S, van Dijken JP, Pronk JT. In Vivo Analysis of the Mechanisms for Oxidation of Cytosolic NADH by Saccharomyces cerevisiae Mitochondria. J Bacteriol. 2000 May 15;182(10):2823–30. doi: 10.1128/jb.182.10.2823-2830.2000.; Luttik MAH, Overkamp KM, Kötter P, de Vries S, van Dijken JP, Pronk JT. The Saccharomyces cerevisiae NDE1 and NDE2 Genes Encode Separate Mitochondrial NADH Dehydrogenases Catalyzing the Oxidation of Cytosolic NADH. Journal of Biological Chemistry. 1998 Sep;273(38):24529–34. doi: 10.1074/jbc.273.38.24529.; Small WC, McAlister-Henn L. Identification of a Cytosolically Directed NADH Dehydrogenase in Mitochondria of Saccharomyces cerevisiae. J Bacteriol. 1998 Aug 15;180(16):4051–5. doi: 10.1128/jb.180.16.4051-4055.1998.; Tessier WD, Meaden PG, Dickinson FM, Midgley M. Identification and disruption of the gene encoding the K(+)-activated acetaldehyde dehydrogenase of Saccharomyces cerevisiae. FEMS Microbiol Lett. 1998 Jul 01;164(1):29–34. doi: 10.1111/j.1574-6968.1998.tb13063.x. PMID: 9675847.; Wang X, Bai Y, Ni L, Weiner H. Saccharomyces cerevisiae aldehyde dehydrogenases. Identification and expression. Adv Exp Med Biol. 1997;414():277–80. doi: 10.1007/978-1-4615-5871-2_32. PMID: 9059631.; DE VRIES S, VAN WITZENBURG R, GRIVELL LA, MARRES CAM. Primary structure and import pathway of the rotenone-insensitive NADH-ubiquinone oxidoreductase of mitochondria from Saccharomyces cerevisiae. European Journal of Biochemistry. 1992 Feb;203(3):587–92. doi: 10.1111/j.1432-1033.1992.tb16587.x.; MARRES CAM, de VRIES S, GRIVELL LA. Isolation and inactivation of the nuclear gene encoding the rotenone-insensitive internal NADH: ubiquinone oxidoreductase of mitochondria from Saccharomyces cerevisiae. European Journal of Biochemistry. 1991 Feb;195(3):857–62. doi: 10.1111/j.1432-1033.1991.tb15775.x.; de VRIES S, GRIVELL LA. Purification and characterization of a rotenone-insensitive NADH: Q6 oxidoreductase from mitochondria of Saccharomyces cerevisiae. European Journal of Biochemistry. 1988 Sep;176(2):377–84. doi: 10.1111/j.1432-1033.1988.tb14292.x.; Bruinenberg PM. The NADP(H) redox couple in yeast metabolism. Antonie Van Leeuwenhoek. 1986;52(5):411–29. doi: 10.1007/bf00393469. PMID: 3789705.

Metabolites

Flavone

Formula: C15H10O2 (222.06807600000002)

CAS ID: 525-82-6

H+

Formula: H (1.0078246)

CAS ID: 12408-02-5

H2O

Formula: H2O (18.0105642)

CAS ID: 7732-18-5

Potassium cation

Formula: K (38.963708)

CAS ID: 24203-36-9

Ubiquinone-1

Formula: C14H18O4 (250.1205028)

CAS ID: 727-81-1

QH(2)

Formula: C14H20O4 (252.136152)

CAS ID: 52590-98-4

NADPH(4-)

Formula: C21H26N7O17P3 (741.0598016)

CAS ID: 53-57-6

ATP(4-)

Formula: C10H12N5O13P3 (502.9644492)

CAS ID:

NAD(1-)

Formula: C21H26N7O14P2 (662.1012936000001)

CAS ID: 53-84-9

ADP(3-)

Formula: C10H12N5O10P2 (424.0059412)

CAS ID:

NADP(3-)

Formula: C21H25N7O17P3 (740.051977)

CAS ID: 53-59-8



Enzyme

EC Number name full name note
1.2.1.-
1.2.1.4 aldehyde dehydrogenase (NADP+) aldehyde:NADP+ oxidoreductase
1.6.5.9 NADH:quinone reductase (non-electrogenic) NADH:quinone oxidoreductase
2.7.1.86 NADH kinase ATP:NADH 2'-phosphotransferase


Proteins

Protein ID name full name
P32340 NDI1 Rotenone-insensitive NADH-ubiquinone oxidoreductase, mitochondrial
P40047 ALD5 Aldehyde dehydrogenase 5, mitochondrial
P40215 NDE1 External NADH-ubiquinone oxidoreductase 1, mitochondrial
Q06892 POS5 NADH kinase POS5, mitochondrial
Q07500 NDE2 External NADH-ubiquinone oxidoreductase 2, mitochondrial