Pathways Knowlegdes
Necessitatibus eius consequatur ex aliquid fuga eum quidem sint consectetur velit
| Pathway | DOIs | Note |
|---|---|---|
| proline to cytochrome bo oxidase electron transfer Accession ID: BioCyc:ECO_PWY0-1544 |
|
Abrahamson JL, Baker LG, Stephenson JT, Wood JM. Proline dehydrogenase from Escherichia coli K12. Properties of the membrane-associated enzyme. Eur J Biochem. 1983 Jul 15;134(1):77–82. doi: 10.1111/j.1432-1033.1983.tb07533.x. PMID: 6305659. |
| pyruvate to cytochrome bd oxidase electron transfer Accession ID: BioCyc:ECO_PWY-7545 |
|
Koland JG, Miller MJ, Gennis RB. Reconstitution of the membrane-bound, ubiquinone-dependent pyruvate oxidase respiratory chain of Escherichia coli with the cytochrome d terminal oxidase. Biochemistry. 1984 Jan 31;23(3):445–53. doi: 10.1021/bi00298a008. PMID: 6367818. |
| pyruvate to cytochrome bo oxidase electron transfer Accession ID: BioCyc:ECO_PWY-7544 |
|
Carter K, Gennis RB. Reconstitution of the Ubiquinone-dependent pyruvate oxidase system of Escherichia coli with the cytochrome o terminal oxidase complex. Journal of Biological Chemistry. 1985 Sep;260(20):10986–90. doi: 10.1016/s0021-9258(17)39135-4. |
| nitric oxide biosynthesis (plants) Accession ID: BioCyc:ARA_PWY-6845 |
|
Guo F, Crawford NM. Arabidopsis Nitric Oxide Synthase1 Is Targeted to Mitochondria and Protects against Oxidative Damage and Dark-Induced Senescence. Plant Cell. 2005 Nov 04;17(12):3436–50. doi: 10.1105/tpc.105.037770.; Guo FQ, Okamoto M, Crawford NM. Identification of a plant nitric oxide synthase gene involved in hormonal signaling. Science. 2003 Oct 03;302(5642):100–3. doi: 10.1126/science.1086770. PMID: 14526079. |
| protein S-nitrosylation and denitrosylation Accession ID: BioCyc:AURANTIMONAS_PWY-7798 |
- | |
| nitrate reduction I (denitrification) Accession ID: BioCyc:SCO_DENITRIFICATION-PWY |
- | |
| nitrate reduction VII (denitrification) Accession ID: BioCyc:META_PWY-6748 |
|
Suharti, Heering HA, de Vries S. NO Reductase fromBacillus azotoformansIs a Bifunctional Enzyme Accepting Electrons from Menaquinol and a Specific Endogenous Membrane-Bound Cytochromec551. Biochemistry. 2004 Oct 01;43(42):13487–95. doi: 10.1021/bi0488101.; Suharti, Strampraad MJ, Schröder I, de Vries S. A novel copper A containing menaquinol NO reductase from Bacillus azotoformans. Biochemistry. 2001 Feb 27;40(8):2632–9. doi: 10.1021/bi0020067. PMID: 11327887.; Cramm R, Pohlmann A, Friedrich B. Purification and characterization of the single-component nitric oxide reductase from Ralstonia eutropha H16. FEBS Lett. 1999 Oct 22;460(1):6–10. doi: 10.1016/s0014-5793(99)01315-0. PMID: 10571051.; Cramm R, Siddiqui RA, Friedrich B. Two isofunctional nitric oxide reductases in Alcaligenes eutrophus H16. J Bacteriol. 1997 Nov;179(21):6769–77. doi: 10.1128/jb.179.21.6769-6777.1997. |
| nitrite reduction (hemoglobin) Accession ID: BioCyc:META_PWY-7683 |
|
Sturms R, DiSpirito AA, Fulton DB, Hargrove MS. Hydroxylamine reduction to ammonium by plant and cyanobacterial hemoglobins. Biochemistry. 2011 Dec 20;50(50):10829–35. doi: 10.1021/bi201425f. PMID: 22080728.; Sturms R, DiSpirito AA, Hargrove MS. Plant and cyanobacterial hemoglobins reduce nitrite to nitric oxide under anoxic conditions. Biochemistry. 2011 May 17;50(19):3873–8. doi: 10.1021/bi2004312. PMID: 21495624. |
| nitrite-dependent anaerobic methane oxidation Accession ID: BioCyc:META_PWY-6523 |
|
Ettwig KF, Butler MK, Le Paslier D, Pelletier E, Mangenot S, Kuypers MMM, Schreiber F, Dutilh BE, Zedelius J, de Beer D, Gloerich J, Wessels HJCT, van Alen T, Luesken F, Wu ML, van de Pas-Schoonen KT, Op den Camp HJM, Janssen-Megens EM, Francoijs K, Stunnenberg H, Weissenbach J, Jetten MSM, Strous M. Nitrite-driven anaerobic methane oxidation by oxygenic bacteria. Nature. 2010 Mar;464(7288):543–8. doi: 10.1038/nature08883. |
| nitric oxide biosynthesis II (mammals) Accession ID: BioCyc:META_PWY-4983 |
|
Nussler AK, Billiar TR, Liu ZZ, Morris SM. Coinduction of nitric oxide synthase and argininosuccinate synthetase in a murine macrophage cell line. Implications for regulation of nitric oxide production. Journal of Biological Chemistry. 1994 Jan;269(2):1257–61. doi: 10.1016/s0021-9258(17)42251-4. |
| D-lactate to cytochrome bo oxidase electron transfer Accession ID: BioCyc:ECO_PWY0-1565 |
|
Matsushita K, Kaback HR. D-lactate oxidation and generation of the proton electrochemical gradient in membrane vesicles from Escherichia coli GR19N and in proteoliposomes reconstituted with purified D-lactate dehydrogenase and cytochrome o oxidase. Biochemistry. 1986 May 06;25(9):2321–7. doi: 10.1021/bi00357a004. PMID: 3013300. |
| NADH to cytochrome bo oxidase electron transfer I Accession ID: BioCyc:ECO_PWY0-1335 |
|
Yagi T, Matsuno-Yagi A. The proton-translocating NADH-quinone oxidoreductase in the respiratory chain: the secret unlocked. Biochemistry. 2003 Mar 04;42(8):2266–74. doi: 10.1021/bi027158b. PMID: 12600193.; Tran QH, Bongaerts J, Vlad D, Unden G. Requirement for the Proton-Pumping NADH Dehydrogenase I of Escherichia Coli in Respiration of NADH to Fumarate and Its Bioenergetic Implications. European Journal of Biochemistry. 1997 Feb;244(1):155–60. doi: 10.1111/j.1432-1033.1997.00155.x.; Calhoun MW, Oden KL, Gennis RB, de Mattos MJ, Neijssel OM. Energetic efficiency of Escherichia coli: effects of mutations in components of the aerobic respiratory chain. J Bacteriol. 1993 May;175(10):3020–5. doi: 10.1128/jb.175.10.3020-3025.1993.; Matsushita K, Ohnishi T, Kaback HR. NADH-ubiquinone oxidoreductases of the Escherichia coli aerobic respiratory chain. Biochemistry. 1987 Dec 01;26(24):7732–7. doi: 10.1021/bi00398a029. PMID: 3122832.; Matsushita K, Kaback HR. D-lactate oxidation and generation of the proton electrochemical gradient in membrane vesicles from Escherichia coli GR19N and in proteoliposomes reconstituted with purified D-lactate dehydrogenase and cytochrome o oxidase. Biochemistry. 1986 May 06;25(9):2321–7. doi: 10.1021/bi00357a004. PMID: 3013300.; Matsushita K, Patel L, Kaback HR. Cytochrome o type oxidase from Escherichia coli. Characterization of the enzyme and mechanism of electrochemical proton gradient generation. Biochemistry. 1984 Sep 25;23(20):4703–14. doi: 10.1021/bi00315a028. PMID: 6093862.; Ingledew WJ, Poole RK. The respiratory chains of Escherichia coli. Microbiol Rev. 1984 Sep;48(3):222–71. doi: 10.1128/mr.48.3.222-271.1984.; Kita K, Kasahara M, Anraku Y. Formation of a Membrane Potential by Reconstituted Liposomes Made with Cytochrome b562-o Complex, a Terminal Oxidase of Escherichia coli*. Journal of Biological Chemistry. 1982 Jul;257(14):7933–5. doi: 10.1016/s0021-9258(18)34273-x. |
| NADH to cytochrome bd oxidase electron transfer I Accession ID: BioCyc:ECO_PWY0-1334 |
|
Unden G, Bongaerts J. Alternative respiratory pathways of Escherichia coli: energetics and transcriptional regulation in response to electron acceptors. Biochimica et Biophysica Acta (BBA) - Bioenergetics. 1997 Jul;1320(3):217–34. doi: 10.1016/s0005-2728(97)00034-0.; Calhoun MW, Oden KL, Gennis RB, de Mattos MJ, Neijssel OM. Energetic efficiency of Escherichia coli: effects of mutations in components of the aerobic respiratory chain. J Bacteriol. 1993 May;175(10):3020–5. doi: 10.1128/jb.175.10.3020-3025.1993.; Puustinen A, Finel M, Haltia T, Gennis RB, Wikström M. Properties of the two terminal oxidases of Escherichia coli. Biochemistry. 1991 Apr 23;30(16):3936–42. doi: 10.1021/bi00230a019. PMID: 1850294.; Cotter PA, Chepuri V, Gennis RB, Gunsalus RP. Cytochrome o (cyoABCDE) and d (cydAB) oxidase gene expression in Escherichia coli is regulated by oxygen, pH, and the fnr gene product. J Bacteriol. 1990 Nov;172(11):6333–8. doi: 10.1128/jb.172.11.6333-6338.1990.; Ingledew WJ, Poole RK. The respiratory chains of Escherichia coli. Microbiol Rev. 1984 Sep;48(3):222–71. doi: 10.1128/mr.48.3.222-271.1984. |
| oxalate degradation V Accession ID: BioCyc:BSUB_PWY-6698 |
- | |
| protein S-nitrosylation and denitrosylation Accession ID: BioCyc:META_PWY-7798 |
|
Hess DT, Matsumoto A, Kim S, Marshall HE, Stamler JS. Protein S-nitrosylation: purview and parameters. Nature Reviews Molecular Cell Biology. 2005 Feb 01;6(2):150–66. doi: 10.1038/nrm1569.; Liu L, Hausladen A, Zeng M, Que L, Heitman J, Stamler JS. A metabolic enzyme for S-nitrosothiol conserved from bacteria to humans. Nature. 2001 Mar 22;410(6827):490–4. doi: 10.1038/35068596. PMID: 11260719.; Jensen DE, Belka GK, Du Bois GC. S-Nitrosoglutathione is a substrate for rat alcohol dehydrogenase class III isoenzyme. Biochem J. 1998 Apr 15;331 ( Pt 2)():659–68. PMID: 9531510; PMCID: PMC1219401. |
| NADH to cytochrome bd oxidase electron transfer II Accession ID: BioCyc:META_PWY0-1568 |
|
Unden G, Bongaerts J. Alternative respiratory pathways of Escherichia coli: energetics and transcriptional regulation in response to electron acceptors. Biochimica et Biophysica Acta (BBA) - Bioenergetics. 1997 Jul;1320(3):217–34. doi: 10.1016/s0005-2728(97)00034-0.; Tran QH, Bongaerts J, Vlad D, Unden G. Requirement for the Proton-Pumping NADH Dehydrogenase I of Escherichia Coli in Respiration of NADH to Fumarate and Its Bioenergetic Implications. European Journal of Biochemistry. 1997 Feb;244(1):155–60. doi: 10.1111/j.1432-1033.1997.00155.x.; Calhoun MW, Oden KL, Gennis RB, de Mattos MJ, Neijssel OM. Energetic efficiency of Escherichia coli: effects of mutations in components of the aerobic respiratory chain. J Bacteriol. 1993 May;175(10):3020–5. doi: 10.1128/jb.175.10.3020-3025.1993.; Cotter PA, Chepuri V, Gennis RB, Gunsalus RP. Cytochrome o (cyoABCDE) and d (cydAB) oxidase gene expression in Escherichia coli is regulated by oxygen, pH, and the fnr gene product. J Bacteriol. 1990 Nov;172(11):6333–8. doi: 10.1128/jb.172.11.6333-6338.1990.; Ingledew WJ, Poole RK. The respiratory chains of Escherichia coli. Microbiol Rev. 1984 Sep;48(3):222–71. doi: 10.1128/mr.48.3.222-271.1984. |
| D-lactate to cytochrome bo oxidase electron transfer Accession ID: BioCyc:META_PWY0-1565 |
|
Matsushita K, Kaback HR. D-lactate oxidation and generation of the proton electrochemical gradient in membrane vesicles from Escherichia coli GR19N and in proteoliposomes reconstituted with purified D-lactate dehydrogenase and cytochrome o oxidase. Biochemistry. 1986 May 06;25(9):2321–7. doi: 10.1021/bi00357a004. PMID: 3013300. |
| proline to cytochrome bo oxidase electron transfer Accession ID: BioCyc:META_PWY0-1544 |
|
Abrahamson JL, Baker LG, Stephenson JT, Wood JM. Proline dehydrogenase from Escherichia coli K12. Properties of the membrane-associated enzyme. Eur J Biochem. 1983 Jul 15;134(1):77–82. doi: 10.1111/j.1432-1033.1983.tb07533.x. PMID: 6305659. |
| NADH to cytochrome bd oxidase electron transfer II Accession ID: BioCyc:ECO_PWY0-1568 |
|
Unden G, Bongaerts J. Alternative respiratory pathways of Escherichia coli: energetics and transcriptional regulation in response to electron acceptors. Biochimica et Biophysica Acta (BBA) - Bioenergetics. 1997 Jul;1320(3):217–34. doi: 10.1016/s0005-2728(97)00034-0.; Tran QH, Bongaerts J, Vlad D, Unden G. Requirement for the Proton-Pumping NADH Dehydrogenase I of Escherichia Coli in Respiration of NADH to Fumarate and Its Bioenergetic Implications. European Journal of Biochemistry. 1997 Feb;244(1):155–60. doi: 10.1111/j.1432-1033.1997.00155.x.; Calhoun MW, Oden KL, Gennis RB, de Mattos MJ, Neijssel OM. Energetic efficiency of Escherichia coli: effects of mutations in components of the aerobic respiratory chain. J Bacteriol. 1993 May;175(10):3020–5. doi: 10.1128/jb.175.10.3020-3025.1993.; Cotter PA, Chepuri V, Gennis RB, Gunsalus RP. Cytochrome o (cyoABCDE) and d (cydAB) oxidase gene expression in Escherichia coli is regulated by oxygen, pH, and the fnr gene product. J Bacteriol. 1990 Nov;172(11):6333–8. doi: 10.1128/jb.172.11.6333-6338.1990.; Ingledew WJ, Poole RK. The respiratory chains of Escherichia coli. Microbiol Rev. 1984 Sep;48(3):222–71. doi: 10.1128/mr.48.3.222-271.1984. |
| NADH to cytochrome bo oxidase electron transfer II Accession ID: BioCyc:ECO_PWY0-1567 |
|
Unden G, Bongaerts J. Alternative respiratory pathways of Escherichia coli: energetics and transcriptional regulation in response to electron acceptors. Biochimica et Biophysica Acta (BBA) - Bioenergetics. 1997 Jul;1320(3):217–34. doi: 10.1016/s0005-2728(97)00034-0.; Tran QH, Bongaerts J, Vlad D, Unden G. Requirement for the Proton-Pumping NADH Dehydrogenase I of Escherichia Coli in Respiration of NADH to Fumarate and Its Bioenergetic Implications. European Journal of Biochemistry. 1997 Feb;244(1):155–60. doi: 10.1111/j.1432-1033.1997.00155.x.; Calhoun MW, Oden KL, Gennis RB, de Mattos MJ, Neijssel OM. Energetic efficiency of Escherichia coli: effects of mutations in components of the aerobic respiratory chain. J Bacteriol. 1993 May;175(10):3020–5. doi: 10.1128/jb.175.10.3020-3025.1993.; Ingledew WJ, Poole RK. The respiratory chains of Escherichia coli. Microbiol Rev. 1984 Sep;48(3):222–71. doi: 10.1128/mr.48.3.222-271.1984. |