Subsystem: Chorismate Synthesis
This subsystem's description is:
For more information, please check out the description and the additional notes tabs, below
Literature References | L-Aspartate semialdehyde and a 6-deoxy-5-ketohexose 1-phosphate are the precursors to the aromatic amino acids in Methanocaldococcus jannaschii. White RH Biochemistry 2004 Jun 15 | 15182204 | Novel benzene ring biosynthesis from C(3) and C(4) primary metabolites by two enzymes. Suzuki H The Journal of biological chemistry 2006 Dec 1 | 17003031 | Biochemical and genetic characterization of an early step in a novel pathway for the biosynthesis of aromatic amino acids and p-aminobenzoic acid in the archaeon Methanococcus maripaludis. Porat I Molecular microbiology 2006 Nov | 17010158 |
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variant code = 1 functional variant, common biochemistry variant code = 2 functional variant, alternative biochemistry variant code = 0 work in progress variant code = -1 no functional variant found Alternative biochemistry published in: Robert H. White. L-Aspartate Semialdehyde and a 6-Deoxy-5-ketohexose 1-Phosphate are the Precursors to the Aromatic Amino Acids in Methanocaldococcus jannaschii. Biochemistry 2004, 43, 7618-7627 Porat I, Sieprawska-Lupa M, Teng Q, Bohanon FJ, White RH, Whitman WB. Biochemical and genetic characterization of an early step in a novel pathway for the biosynthesis of aromatic amino acids and p-aminobenzoic acid in the archaeon Methanococcus maripaludis. Mol Microbiol. 2006 Nov;62(4):1117-31. Epub 2006 Sep 29. ------------------------------------------------------------------------------- 272557.1 Aeropyrum pernix K1 does not seem to have a PDH 273063.1 Sulfolobus tokadaii lost peg 323 with PDH needs 'recreation' 2208.1 Methanosarcina barkeri CM gene not called located between 1823 and 1824 272844.1 Pyrococcus abyssi GE5 has a deletion between peg 477 and peg 478 of CM, aminotransferase and PDG genes compared to Pyrococcus furiosus DSM 3638 and others. No other instances of those genes found in genome. 1308.2 Streptococcus thermophilus ACTT BAA-491 has a diverging duplication of the cluster need to check what each of them does 68909.1 Deinococcus geothermalis DSM11300 SK ORF not called Check fig|205921.3.peg.1687 Streptomyces have 3 CM fig|227882.1.peg.6212 MTNSNTRTGTGDVDPAVRAELARLRDSIDNIDAA----VVHMLAERFKCT fig|227882.1.peg.5022 MAEVLDRTGARTVEAAD--VISGARERIDSLDDR----IIGLVQERMAVS fig|227882.1.peg.6522 MAVRAVRGAVQLERDAADHMDEQVSELLTAILERNGLTADDLISIWFTAT *: * .. * : : : :: : : fig|227882.1.peg.6212 QQVGHLKAVHQLPPADPAREASQIARLRRLAENAKLDPAFAEKLLGFIIA fig|227882.1.peg.5022 AVIQEARIASGGRRVNLSREMEVLGHFRDALG----KPG---TSLAMTLL fig|227882.1.peg.6522 PDLHSDFPAAAARKLGIVDVPLICAQELDIKG----AMPRVVRVLAHIES : . . .: *. fig|227882.1.peg.6212 EVIRHHERIADNTANGSVSAPPATEDDTTGPAE fig|227882.1.peg.5022 ELCR-----------GRI--------------- fig|227882.1.peg.6522 DKPRAEIAHVYLGAAGALRKDIAQ--------- : * * : DAHPS - "The biosynthetic reaction is a condensation of P-enolpyruvate and D-erythrose-4-P to form orthophosphate and 3-deoxy-D-arabino-heptulosonate 7-phosphate. The latter designation has been used in accordance with both the Carbohydrate Committee rules and Chemical Abstracts usage since 1960. However, the Enzyme Commission has adopted a different systemic name (7-phospho-2-oxo-3-deoxy-D-arabino-heptonate D-erythrose-4-phosphate-lyase (pyruvate phosphorylating), EC 4.1.2.15) and recommemded the use of the trivial name, phospho-2-keto-3-deoxyheptonate aldolase. In spite of the fact that the reaction catalyzed by 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase is irreversible, the E.C. name is based upon the reverse reaction. It is also clear that the reaction is not an aldol condensation. The E.C. name is further inappropriate because of the implication that pyruvate would be phosphorylated, even though pyruvate is not a participant in the reaction." Currently selected organism: Anabaena variabilis ATCC 29413 (open scenarios overview page for organism)
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