Pathways Knowlegdes

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Pathway DOIs Note
N10-formyl-tetrahydrofolate biosynthesis

Accession ID: BioCyc:META_1CMET2-PWY
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(S,S)-butanediol biosynthesis

Accession ID: BioCyc:META_PWY-6390
  • 10.1111/j.1432-1033.1991.tb16019.x
CARBALLO J, MARTIN R, BERNARDO A, GONZALEZ J. Purification, characterization and some properties of diacetyl(acetoin) reductase from Enterobacter aerogenes. European Journal of Biochemistry. 1991 Jun;198(2):327–32. doi: 10.1111/j.1432-1033.1991.tb16019.x.
superpathway of 2,3-butanediol biosynthesis

Accession ID: BioCyc:META_PWY-6396
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adenine and adenosine salvage III

Accession ID: BioCyc:META_PWY-6609
  • 10.1016/s0163-7258(00)00097-8
  • 10.1016/s0944-5013(11)80008-x
Bzowska A, Kulikowska E, Shugar D. Purine nucleoside phosphorylases: properties, functions, and clinical aspects. Pharmacol Ther. 2000 Dec;88(3):349–425. doi: 10.1016/s0163-7258(00)00097-8. PMID: 11337031.; Elshafei AM, Abu-Shady MR, el-Beih FM, Mohamed LA. Mode and extent of degradation of adenosine and guanosine by extracts of Aspergillus terricola. Microbiol Res. 1995 Sep;150(3):291–5. doi: 10.1016/s0944-5013(11)80008-x. PMID: 7551735.
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 tetrahydrofolate biosynthesis

Accession ID: BioCyc:ECO_PWY-6612
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heparin degradation

Accession ID: BioCyc:META_PWY-7644
  • 10.1016/s0021-9258(19)43461-3
  • 10.1128/aem.62.8.2723-2734.1996
Su H, Blain F, Musil RA, Zimmermann JJ, Gu K, Bennett DC. Isolation and expression in Escherichia coli of hepB and hepC, genes coding for the glycosaminoglycan-degrading enzymes heparinase II and heparinase III, respectively, from Flavobacterium heparinum. Appl Environ Microbiol. 1996 Aug;62(8):2723–34. doi: 10.1128/aem.62.8.2723-2734.1996.; Dietrich CP, Silva ME, Michelacci YM. Sequential degradation of heparin in Flavobacterium heparinum. Purification and properties of five enzymes involved in heparin degradation. J Biol Chem. 1973 Sep 25;248(18):6408–15. PMID: 4730325.
superpathway of tetrahydrofolate biosynthesis

Accession ID: BioCyc:META_PWY-6612
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nitrilotriacetate degradation

Accession ID: BioCyc:META_PWY-6021
  • 10.1007/s10532-007-9113-y
  • 10.1016/s1389-1723(01)80207-3
  • 10.1128/jb.174.4.1179-1188.1992
  • 10.1128/jb.178.21.6123-6132.1996
  • 10.1128/jb.179.4.1112-1116.1997
Yuan Z, VanBriesen JM. Bacterial growth yields on EDTA, NTA, and their biodegradation intermediates. Biodegradation. 2008 Feb;19(1):41–52. doi: 10.1007/s10532-007-9113-y. PMID: 17404695.; Egli T. Biodegradation of metal-complexing aminopolycarboxylic acids. Journal of Bioscience and Bioengineering. 2001 Jan;92(2):89–97. doi: 10.1016/s1389-1723(01)80207-3.; Xu Y, Mortimer MW, Fisher TS, Kahn ML, Brockman FJ, Xun L. Cloning, sequencing, and analysis of a gene cluster from Chelatobacter heintzii ATCC 29600 encoding nitrilotriacetate monooxygenase and NADH:flavin mononucleotide oxidoreductase. J Bacteriol. 1997 Feb;179(4):1112–6. doi: 10.1128/jb.179.4.1112-1116.1997.; Knobel HR, Egli T, van der Meer JR. Cloning and characterization of the genes encoding nitrilotriacetate monooxygenase of Chelatobacter heintzii ATCC 29600. J Bacteriol. 1996 Nov;178(21):6123–32. doi: 10.1128/jb.178.21.6123-6132.1996.; Uetz T, Schneider R, Snozzi M, Egli T. Purification and characterization of a two-component monooxygenase that hydroxylates nitrilotriacetate from 'Chelatobacter' strain ATCC 29600. J Bacteriol. 1992 Feb;174(4):1179–88. doi: 10.1128/jb.174.4.1179-1188.1992.
(S,S)-butanediol degradation

Accession ID: BioCyc:META_PWY-6388
  • 10.1271/bbb.65.1876
TAKUSAGAWA Y, OTAGIRI M, UI S, OHTSUKI T, MIMURA A, OHKUMA M, KUDO T. Purification and Characterization of L-2,3-Butanediol Dehydrogenase of Brevibacterium saccharolyticum C-1012 Expressed in Escherichia coli. Bioscience, Biotechnology, and Biochemistry. 2001 Jan;65(8):1876–8. doi: 10.1271/bbb.65.1876.
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.
L-lysine degradation IV

Accession ID: BioCyc:META_PWY-5280
  • 10.1016/s0021-9258(18)61968-4
  • 10.1016/s0021-9258(19)42770-1
  • 10.1128/jb.117.2.753-764.1974
  • 10.1128/jb.187.21.7500-7510.2005
Revelles O, Espinosa-Urgel M, Fuhrer T, Sauer U, Ramos JL. Multiple and Interconnected Pathways for l -Lysine Catabolism in Pseudomonas putida KT2440. J Bacteriol. 2005 Nov;187(21):7500–10. doi: 10.1128/jb.187.21.7500-7510.2005.; 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.; Flashner MIS, Massey V. Purification and Properties of l-Lysine Monooxygenase from Pseudomonas fluorescens. Journal of Biological Chemistry. 1974 Apr;249(8):2579–86. doi: 10.1016/s0021-9258(19)42770-1.; Chang Y, Adams E. d -Lysine Catabolic Pathway in Pseudomonas putida: Interrelations with l -Lysine Catabolism. J Bacteriol. 1974 Feb;117(2):753–64. doi: 10.1128/jb.117.2.753-764.1974.; Miller DL, Rodwell VW. Metabolism of basic amino acids in Pseudomonas putida. Catabolism of lysine by cyclic and acyclic intermediates. J Biol Chem. 1971 May 10;246(9):2758–64. PMID: 5554291.
tetrahydrofolate biosynthesis

Accession ID: BioCyc:META_PWY-6614
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adenine and adenosine salvage III

Accession ID: BioCyc:ECO_PWY-6609
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N10-formyl-tetrahydrofolate biosynthesis

Accession ID: BioCyc:ECO_1CMET2-PWY
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tetrahydrofolate biosynthesis

Accession ID: BioCyc:ECO_PWY-6614
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superpathway of tetrahydrofolate biosynthesis and salvage

Accession ID: BioCyc:META_FOLSYN-PWY
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superpathway of chorismate metabolism

Accession ID: BioCyc:ECO_ALL-CHORISMATE-PWY
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15q11q13 copy number variation

Accession ID: WikiPathways:WP5407
  • 10.1074/jbc.c000302200
Lee D, Tomita S, Kirino Y, Suzuki T. Regulation of X11L-dependent Amyloid Precursor Protein Metabolism by XB51, a Novel X11L-binding Protein. Journal of Biological Chemistry. 2000 Jul;275(30):23134–8. doi: 10.1074/jbc.c000302200.