Pathways Knowlegdes

Necessitatibus eius consequatur ex aliquid fuga eum quidem sint consectetur velit


Pathway DOIs Note
superpathway of L-phenylalanine biosynthesis

Accession ID: BioCyc:META_PWY-6628
  • 10.1016/s0021-9258(17)32929-0
Weigent DA, Nester EW. Purification and properties of two aromatic aminotransferases in Bacillus subtilis. Journal of Biological Chemistry. 1976 Nov;251(22):6974–80. doi: 10.1016/s0021-9258(17)32929-0.
L-lysine fermentation to acetate and butanoate

Accession ID: BioCyc:META_P163-PWY
  • 10.1016/s0021-9258(18)65732-1
  • 10.1016/s0021-9258(18)71290-8
  • 10.1016/s0021-9258(18)71291-x
  • 10.1016/s0021-9258(18)94472-8
  • 10.1016/s0021-9258(18)96751-7
  • 10.1021/bi00730a006
  • 10.1021/bi020255k
  • 10.1096/fasebj.9.9.7601336
  • 10.1099/00207713-50-3-1259
  • 10.1128/jb.152.1.201-207.1982
  • 10.1128/jb.182.2.469-476.2000
Tang KH, Harms A, Frey PA. Identification of a novel pyridoxal 5'-phosphate binding site in adenosylcobalamin-dependent lysine 5,6-aminomutase from Porphyromonas gingivalis. Biochemistry. 2002 Jul 09;41(27):8767–76. doi: 10.1021/bi020255k. PMID: 12093296.; Mechichi T, Fardeau ML, Labat M, Garcia JL, Verhé F, Patel BK. Clostridium peptidivorans sp. nov., a peptide-fermenting bacterium from an olive mill wastewater treatment digester. Int J Syst Evol Microbiol. 2000 May;50 Pt 3():1259–64. doi: 10.1099/00207713-50-3-1259. PMID: 10843071.; Ruzicka FJ, Lieder KW, Frey PA. Lysine 2,3-Aminomutase from Clostridium subterminale SB4: Mass Spectral Characterization of Cyanogen Bromide-Treated Peptides and Cloning, Sequencing, and Expression of the Gene kamA in Escherichia coli. J Bacteriol. 2000 Jan 15;182(2):469–76. doi: 10.1128/jb.182.2.469-476.2000.; Thorpe C, Kim JP. Structure and mechanism of action of the Acyl-CoA dehydrogenases 1. The FASEB Journal. 1995 Jun;9(9):718–25. doi: 10.1096/fasebj.9.9.7601336.; Barker HA, Kahn JM, Hedrick L. Pathway of lysine degradation in Fusobacterium nucleatum. J Bacteriol. 1982 Oct;152(1):201–7. doi: 10.1128/jb.152.1.201-207.1982.; Baker JJ, van der Drift C, Stadtman TC. Purification and properties of -lysine mutase, a pyridoxal phosphate and B 12 coenzyme dependent enzyme. Biochemistry. 1973 Mar 13;12(6):1054–63. doi: 10.1021/bi00730a006. PMID: 4540127.; Chirpich TP, Zappia V, Costilow RN, Barker HA. Lysine 2,3-aminomutase. Purification and properties of a pyridoxal phosphate and S-adenosylmethionine-activated enzyme. J Biol Chem. 1970 Apr 10;245(7):1778–89. PMID: 5438361.; Rimerman EA, Barker HA. Formation and Identification of 3-Keto-5-aminohexanoic Acid, a Probable Intermediate in Lysine Fermentation. Journal of Biological Chemistry. 1968 Dec;243(23):6151–60. doi: 10.1016/s0021-9258(18)94472-8.; Costilow RN, Rochovansky OM, Barker HA. Isolation and Identification of ß-Lysine as an Intermediate in Lysine Fermentation. Journal of Biological Chemistry. 1966 Apr;241(7):1573–80. doi: 10.1016/s0021-9258(18)96751-7.; Hauge JG, Crane FL, Beinert H. ON THE MECHANISM OF DEHYDROGENATION OF FATTY ACYL DERIVATIVES OF COENZYME A. Journal of Biological Chemistry. 1956 Apr;219(2):727–33. doi: 10.1016/s0021-9258(18)65732-1.; Green DE, Mii S, Mahler HR, Bock RM. STUDIES ON THE FATTY ACID OXIDIZING SYSTEM OF ANIMAL TISSUES. Journal of Biological Chemistry. 1954 Jan;206(1):1–12. doi: 10.1016/s0021-9258(18)71290-8.; MAHLER HR. Studies on the fatty acid oxidizing system of animal tissues. IV. The prosthetic group of butyryl coenzyme A dehydrogenase. J Biol Chem. 1954 Jan;206(1):13–26. PMID: 13130522.
L-aspartate degradation I

Accession ID: BioCyc:META_ASPARTATE-DEG1-PWY
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superpathway of chorismate metabolism

Accession ID: BioCyc:META_ALL-CHORISMATE-PWY
  • 10.1021/bi0016523
Keating TA, Marshall CG, Walsh CT. Reconstitution and characterization of the Vibrio cholerae vibriobactin synthetase from VibB, VibE, VibF, and VibH. Biochemistry. 2000 Dec 19;39(50):15522–30. doi: 10.1021/bi0016523. PMID: 11112538.
superpathway of aromatic amino acid biosynthesis

Accession ID: BioCyc:ECO_COMPLETE-ARO-PWY
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superpathway of L-tyrosine biosynthesis

Accession ID: BioCyc:META_PWY-6630
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L-arginine degradation (Stickland reaction)

Accession ID: BioCyc:META_ARGORNPROST-PWY
  • 10.1099/13500872-145-4-819
Kenklies J, Ziehn R, Fritsche K, Pich A, Andreesen JR. Proline biosynthesis from L-ornithine in Clostridium sticklandii: purification of delta1-pyrroline-5-carboxylate reductase, and sequence and expression of the encoding gene, proC. Microbiology (Reading). 1999 Apr;145 ( Pt 4)():819–26. doi: 10.1099/13500872-145-4-819. PMID: 10220161.
mimosine biosynthesis

Accession ID: BioCyc:META_PWY-4985
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chorismate biosynthesis I

Accession ID: BioCyc:ECO_ARO-PWY
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β-alanine biosynthesis III

Accession ID: BioCyc:META_PWY-5155
  • 10.1128/jb.01784-14
  • 10.1128/jb.141.3.1291-1297.1980
Wang Y, Xu H, White RH. ß-alanine biosynthesis in Methanocaldococcus jannaschii. J Bacteriol. 2014 Aug;196(15):2869–75. PMID: 24891443; PMCID: PMC4135672.; Cronan JE. Beta-alanine synthesis in Escherichia coli. J Bacteriol. 1980 Mar;141(3):1291–7. doi: 10.1128/jb.141.3.1291-1297.1980.
superpathway of L-lysine degradation

Accession ID: BioCyc:META_PWY-5327
  • 10.1016/s0021-9258(18)65732-1
  • 10.1016/s0021-9258(18)71290-8
  • 10.1016/s0021-9258(18)71291-x
  • 10.1039/a801345d
  • 10.1096/fasebj.9.9.7601336
Zabriskie TM, Jackson MD. Lysine biosynthesis and metabolism in fungi. Nat Prod Rep. 2000 Feb;17(1):85–97. doi: 10.1039/a801345d. PMID: 10714900.; Thorpe C, Kim JP. Structure and mechanism of action of the Acyl-CoA dehydrogenases 1. The FASEB Journal. 1995 Jun;9(9):718–25. doi: 10.1096/fasebj.9.9.7601336.; Deana R. Substrate specificity of a dicarboxyl-CoA: dicarboxylic acid coenzyme A transferase from rat liver mitochondria. Biochem Int. 1992 Mar;26(4):767–73. PMID: 1610380.; Hauge JG, Crane FL, Beinert H. ON THE MECHANISM OF DEHYDROGENATION OF FATTY ACYL DERIVATIVES OF COENZYME A. Journal of Biological Chemistry. 1956 Apr;219(2):727–33. doi: 10.1016/s0021-9258(18)65732-1.; Green DE, Mii S, Mahler HR, Bock RM. STUDIES ON THE FATTY ACID OXIDIZING SYSTEM OF ANIMAL TISSUES. Journal of Biological Chemistry. 1954 Jan;206(1):1–12. doi: 10.1016/s0021-9258(18)71290-8.; MAHLER HR. Studies on the fatty acid oxidizing system of animal tissues. IV. The prosthetic group of butyryl coenzyme A dehydrogenase. J Biol Chem. 1954 Jan;206(1):13–26. PMID: 13130522.
superpathway of coenzyme A biosynthesis I (bacteria)

Accession ID: BioCyc:META_PANTOSYN-PWY
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lactose and galactose degradation I

Accession ID: BioCyc:META_LACTOSECAT-PWY
  • 10.1016/0006-291x(73)90761-4
  • 10.1016/s0021-9258(18)43562-4
  • 10.1016/s0021-9258(18)43563-6
  • 10.1016/s0021-9258(18)43564-8
  • 10.1073/pnas.58.1.274
Bissett DL, Wenger WC, Anderson RL. Lactose and D-galactose metabolism in Staphylococcus aureus. II. Isomerization of D-galactose 6-phosphate to D-tagatose 6-phosphate by a specific D-galactose-6-phosphate isomerase. Journal of Biological Chemistry. 1980 Sep;255(18):8740–4. doi: 10.1016/s0021-9258(18)43562-4.; Bissett DL, Anderson RL. Lactose and D-galactose metabolism in Staphylococcus aureus. IV. Isolation and properties of a class I D-ketohexose-1,6-diphosphate aldolase that catalyzes the cleavage of D-tagatose 1,6-diphosphate. Journal of Biological Chemistry. 1980 Sep;255(18):8750–5. doi: 10.1016/s0021-9258(18)43564-8.; Bissett DL, Anderson RL. Lactose and D-galactose metabolism in Staphylococcus aureus. III. Purification and properties of D-tagatose-6-phosphate kinase. Journal of Biological Chemistry. 1980 Sep;255(18):8745–9. doi: 10.1016/s0021-9258(18)43563-6.; Bissett DL, Anderson RL. Lactose and D-galactose metabolism in Staphylococcus aureus: Pathway of D-galactose 6-phosphate degradation. Biochemical and Biophysical Research Communications. 1973 May;52(2):641–7. doi: 10.1016/0006-291x(73)90761-4.; Hengstenberg W, Egan JB, Morse ML. Carbohydrate transport in Staphylococcus aureus. V. The accumulation of phosphorylated carbohydrate derivatives, and evidence for a new enzyme-splitting lactose phosphate. Proc Natl Acad Sci U S A. 1967 Jul;58(1):274–9. PMID: 4292101; PMCID: PMC335629.
superpathway of aromatic amino acid biosynthesis

Accession ID: BioCyc:META_COMPLETE-ARO-PWY
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chorismate biosynthesis I

Accession ID: BioCyc:META_ARO-PWY
  • 10.3109/10409239009090615
Bentley R, Haslam E. The Shikimate Pathway — A Metabolic Tree with Many Branche. Critical Reviews in Biochemistry and Molecular Biology. 1990 Jan;25(5):307–84. doi: 10.3109/10409239009090615.
cyanide detoxification I

Accession ID: BioCyc:META_ASPSYNII-PWY
  • 10.1002/9780470513712.ch7
  • 10.1007/s11103-005-6217-9
  • 10.1016/0003-9861(72)90193-2
  • 10.1073/pnas.72.4.1617
  • 10.1073/pnas.81.10.3059
  • 10.1074/jbc.m007890200
  • 10.1093/jxb/ern089
  • 10.1093/pcp/41.4.465
  • 10.1104/pp.110.162412
  • 10.1104/pp.123.3.1163
  • 10.18388/abp.2002_3784
Seo S, Mitsuhara I, Feng J, Iwai T, Hasegawa M, Ohashi Y. Cyanide, a coproduct of plant hormone ethylene biosynthesis, contributes to the resistance of rice to blast fungus. Plant Physiol. 2011 Jan;155(1):502–14. PMID: 21075959; PMCID: PMC3075767.; Oracz K, El-Maarouf-Bouteau H, Bogatek R, Corbineau F, Bailly C. Release of sunflower seed dormancy by cyanide: cross-talk with ethylene signalling pathway. Journal of Experimental Botany. 2008 May 01;59(8):2241–51. doi: 10.1093/jxb/ern089.; Manning K. Detoxification of cyanide by plants and hormone action. Ciba Found Symp. 1988;140():92–110. doi: 10.1002/9780470513712.ch7. PMID: 3073064.; Piotrowski M, Volmer JJ. Cyanide metabolism in higher plants: cyanoalanine hydratase is a NIT4 homolog. Plant Mol Biol. 2006 May;61(1-2):111–22. doi: 10.1007/s11103-005-6217-9. PMID: 16786295.; Jakubowicz M. Structure, catalytic activity and evolutionary relationships of 1-aminocyclopropane-1-carboxylate synthase, the key enzyme of ethylene synthesis in higher plants. Acta Biochim Pol. 2002 Sep 30;49(3):757–74. doi: 10.18388/abp.2002_3784.; Piotrowski M, Schönfelder S, Weiler EW. The Arabidopsis thaliana isogene NIT4 and its orthologs in tobacco encode beta-cyano-L-alanine hydratase/nitrilase. J Biol Chem. 2001 Jan 26;276(4):2616–21. doi: 10.1074/jbc.m007890200. PMID: 11060302.; Hatzfeld Y, Maruyama A, Schmidt A, Noji M, Ishizawa K, Saito K. beta-Cyanoalanine synthase is a mitochondrial cysteine synthase-like protein in spinach and Arabidopsis. Plant Physiol. 2000 Jul;123(3):1163–71. PMID: 10889265; PMCID: PMC59079.; Yamaguchi Y, Nakamura T, Kusano T, Sano H. Three Arabidopsis genes encoding proteins with differential activities for cysteine synthase and beta-cyanoalanine synthase. Plant Cell Physiol. 2000 Apr;41(4):465–76. doi: 10.1093/pcp/41.4.465. PMID: 10845460.; Peiser GD, Wang TT, Hoffman NE, Yang SF, Liu HW, Walsh CT. Formation of cyanide from carbon 1 of 1-aminocyclopropane-1-carboxylic acid during its conversion to ethylene. Proc Natl Acad Sci U S A. 1984 May;81(10):3059–63. PMID: 16593463; PMCID: PMC345220.; Akopyan TN, Braunstein AE, Goryachenkova EV. Beta-cyanoalanine synthase: purification and characterization. Proc. Natl. Acad. Sci. U.S.A. 1975 Apr;72(4):1617–21. doi: 10.1073/pnas.72.4.1617.; Castric PA, Farnden KJ, Conn EE. Cyanide metabolism in higher plants. V. The formation of asparagine from -cyanoalanine. Arch Biochem Biophys. 1972 Sep;152(1):62–9. doi: 10.1016/0003-9861(72)90193-2. PMID: 4627358.
L-ornithine degradation II (Stickland reaction)

Accession ID: BioCyc:META_PWY-6344
  • 10.1099/13500872-145-4-819
Kenklies J, Ziehn R, Fritsche K, Pich A, Andreesen JR. Proline biosynthesis from L-ornithine in Clostridium sticklandii: purification of delta1-pyrroline-5-carboxylate reductase, and sequence and expression of the encoding gene, proC. Microbiology (Reading). 1999 Apr;145 ( Pt 4)():819–26. doi: 10.1099/13500872-145-4-819. PMID: 10220161.
L-arginine degradation X (arginine monooxygenase pathway)

Accession ID: BioCyc:META_ARGDEG-V-PWY
  • 10.1016/0006-3002(56)90230-x
Nguyen Van Thoai, Thome-Beau F, Olomucki A. [Induction and specificity of enzymes of the new catabolic arginine pathway]. Biochim Biophys Acta. 1966 Jan 25;115(1):73–80. PMID: 5936244.; HATT JL, THI AN, VAN THOAI N. [Metabolism of guanidine derivatives. V. Enzymic oxidation of arginine to guanidinobutyramide]. Biochim Biophys Acta. 1956 Oct;22(1):116–23. doi: 10.1016/0006-3002(56)90230-x. PMID: 13373855.
gallate biosynthesis

Accession ID: BioCyc:META_PWY-6707
  • 10.1007/s11103-011-9739-3
Muir RM, Ibáñez AM, Uratsu SL, Ingham ES, Leslie CA, McGranahan GH, Batra N, Goyal S, Joseph J, Jemmis ED, Dandekar AM. Mechanism of gallic acid biosynthesis in bacteria (Escherichia coli) and walnut (Juglans regia). Plant Molecular Biology. 2011 Jan 30;75(6):555–65. doi: 10.1007/s11103-011-9739-3.
tetrapyrrole biosynthesis I (from glutamate)

Accession ID: BioCyc:ECO_PWY-5188
  • 10.1016/0968-0004(90)90304-t
Warren MJ, Scott AI. Tetrapyrrole assembly and modification into the ligands of biologically functional cofactors. Trends Biochem Sci. 1990 Dec;15(12):486–91. doi: 10.1016/0968-0004(90)90304-t. PMID: 2077690.