This view shows enzymes only for those organisms listed below, in the list of taxa known to possess the pathway. If an enzyme name is shown in bold, there is experimental evidence for this enzymatic activity.
|Superclasses:||Degradation/Utilization/Assimilation → Aromatic Compounds Degradation → Quinate Degradation|
L-quinate is a naturally occuring compound found in decaying plant matter [Hawkins93]. Quinate is one of several aromatic compounds that can be metabolized by microorganisms to the central intermediate protocatechuate that can be further metabolized via the β-ketoadipate pathway to acetyl-CoA and succinyl-CoA [Tresguerres70, Adachi03]. Bacteria capable of using quinate as a sole carbon source were observed as early as 1911 [Beijerinck11]
Quinate degradation was initially studied in the fungus Neurospora crassa [Tatum54], and later in other fungi (such as Aspergillus nidulans [Hawkins85]) and bacteria, including Acinetobacter sp. ADP1 (at the time reported as Acinetobacter calcoaceticus) [Elsemore95, Elsemore94], Gluconobacter oxydans [Adachi03] and Corynebacterium glutamicum [Schoepe08].| Many of these organisms can grow on quinate as a sole carbon and energy source, and the pathway is inducible by growth on either L-quinate, shikimate, or protocatechuate.
Two variants of this pathway are present in MetaCyc; the main difference between them lies in the enzyme that catalyzes the initial oxidation of L-quinate. Filamentous fungi and Gram-positive bacteria use an NAD(P)-dependent enzyme (EC 188.8.131.52), while Gram-negative bacteria use a pyrroloquinoline quinone (PQQ)-dependent enzyme (EC 184.108.40.206) [vanKleef88]. The later pathway is desribed in quinate degradation I.
About This Pathway
Quinate degradation was first studied in filamentous fungi such as Neurospora crassa and Aspergillus nidulans. The fungal pathway starts with conversion of L-quinate to 3-dehydroquinate by an NAD-dependent quinate/shikimate dehydrogenase (EC 220.127.116.11). The genes involved in the fungal pathway (qa genes in Neurospora crassa, qut genes in Aspergillus nidulans ) were shown to be present in a single cluster, and are induced by growth on either L-quinate or shikimate [Patel81, Wheeler96, Hawkins93]. The clusters include a gene encoding a permease that enables L-quinate to enter the organism [Whittington87].
An NAD-dependent enzyme is also present in certain Gram-positive bacteria, such as Corynebacterium glutamicum [Teramoto09]. As in the fungi, the qsuD gene, which encodes the Corynebacterium glutamicum enzyme, is located in a gene cluster that also contains the genes encoding the rest of the pathway's enzymes. The cluster, which is under the control of the QsuR regulator, is induced by growth on L-quinate shikimate [Teramoto09].
Variants: quinate degradation I
Adachi03: Adachi O, Tanasupawat S, Yoshihara N, Toyama H, Matsushita K (2003). "3-dehydroquinate production by oxidative fermentation and further conversion of 3-dehydroquinate to the intermediates in the shikimate pathway." Biosci Biotechnol Biochem 67(10);2124-31. PMID: 14586099
Elsemore94: Elsemore DA, Ornston LN (1994). "The pca-pob supraoperonic cluster of Acinetobacter calcoaceticus contains quiA, the structural gene for quinate-shikimate dehydrogenase." J Bacteriol 1994;176(24);7659-66. PMID: 8002591
Hawkins85: Hawkins AR, Francisco Da Silva AJ, Roberts CF (1985). "Cloning and characterization of the three enzyme structural genes QUTB, QUTC and QUTE from the quinic acid utilization gene cluster in Aspergillus nidulans." Curr Genet 9(4);305-11. PMID: 3916726
Hawkins93: Hawkins AR, Lamb HK, Moore JD, Charles IG, Roberts CF (1993). "The pre-chorismate (shikimate) and quinate pathways in filamentous fungi: theoretical and practical aspects." J Gen Microbiol 139(12);2891-9. PMID: 8126417
Patel81: Patel VB, Schweizer M, Dykstra CC, Kushner SR, Giles NH (1981). "Genetic organization and transcriptional regulation in the qa gene cluster of Neurospora crassa." Proc Natl Acad Sci U S A 78(9);5783-7. PMID: 6458044
Schoepe08: Schoepe J, Niefind K, Schomburg D (2008). "1.6 angstroms structure of an NAD+-dependent quinate dehydrogenase from Corynebacterium glutamicum." Acta Crystallogr D Biol Crystallogr D64(Pt 7);803-9. PMID: 18566515
Teramoto09: Teramoto H, Inui M, Yukawa H (2009). "Regulation of expression of genes involved in quinate and shikimate utilization in Corynebacterium glutamicum." Appl Environ Microbiol 75(11);3461-8. PMID: 19376919
Whittington87: Whittington HA, Grant S, Roberts CF, Lamb H, Hawkins AR (1987). "Identification and isolation of a putative permease gene in the quinic acid utilization (QUT) gene cluster of Aspergillus nidulans." Curr Genet 12(2);135-9. PMID: 2835177
Adachi08: Adachi O, Ano Y, Toyama H, Matsushita K (2008). "A novel 3-dehydroquinate dehydratase catalyzing extracellular formation of 3-dehydroshikimate by oxidative fermentation of Gluconobacter oxydans IFO 3244." Biosci Biotechnol Biochem 72(6);1475-82. PMID: 18540103
BSUB93: "Bacillus subtilis and Other Gram-Positive Bacteria: Biochemistry, Physiology, and Molecular Genetics." (1993). Editors: Sonenshein, A.L., Hoch, J.A., Losick, R. American Society For Microbiology, Washington, DC.
Duncan86a: Duncan K, Chaudhuri S, Campbell MS, Coggins JR (1986). "The overexpression and complete amino acid sequence of Escherichia coli 3-dehydroquinase." Biochem J 1986;238(2);475-83. PMID: 3541912
Euverink92: Euverink GJ, Hessels GI, Vrijbloed JW, Coggins JR, Dijkhuizen L (1992). "Purification and characterization of a dual function 3-dehydroquinate dehydratase from Amycolatopsis methanolica." J Gen Microbiol 138(11);2449-57. PMID: 1479361
Geever89: Geever RF, Huiet L, Baum JA, Tyler BM, Patel VB, Rutledge BJ, Case ME, Giles NH (1989). "DNA sequence, organization and regulation of the qa gene cluster of Neurospora crassa." J Mol Biol 207(1);15-34. PMID: 2525625
Hawkins88: Hawkins AR, Lamb HK, Smith M, Keyte JW, Roberts CF (1988). "Molecular organisation of the quinic acid utilization (QUT) gene cluster in Aspergillus nidulans." Mol Gen Genet 214(2);224-31. PMID: 2976880
Hawkins93a: Hawkins AR, Moore JD, Adeokun AM (1993). "Characterization of the 3-dehydroquinase domain of the pentafunctional AROM protein, and the quinate dehydrogenase from Aspergillus nidulans, and the overproduction of the type II 3-dehydroquinase from neurospora crassa." Biochem J 296 ( Pt 2);451-7. PMID: 8257437
Kleanthous92: Kleanthous C, Deka R, Davis K, Kelly SM, Cooper A, Harding SE, Price NC, Hawkins AR, Coggins JR (1992). "A comparison of the enzymological and biophysical properties of two distinct classes of dehydroquinase enzymes." Biochem J 282 ( Pt 3);687-95. PMID: 1554351
Lim02: Lim EK, Doucet CJ, Li Y, Elias L, Worrall D, Spencer SP, Ross J, Bowles DJ (2002). "The activity of Arabidopsis glycosyltransferases toward salicylic acid, 4-hydroxybenzoic acid, and other benzoates." J Biol Chem 277(1);586-92. PMID: 11641410
MITSUHASHI54: MITSUHASHI S, DAVIS BD (1954). "Aromatic biosynthesis. XII. Conversion of 5-dehydroquinic acid to 5-dehydroshikimic acid dy 5-dehydroquinase." Biochim Biophys Acta 15(1);54-61. PMID: 13198937
Pfleger08: Pfleger BF, Kim Y, Nusca TD, Maltseva N, Lee JY, Rath CM, Scaglione JB, Janes BK, Anderson EC, Bergman NH, Hanna PC, Joachimiak A, Sherman DH (2008). "Structural and functional analysis of AsbF: origin of the stealth 3,4-dihydroxybenzoic acid subunit for petrobactin biosynthesis." Proc Natl Acad Sci U S A 105(44);17133-8. PMID: 18955706
Singh06a: Singh SA, Christendat D (2006). "Structure of Arabidopsis dehydroquinate dehydratase-shikimate dehydrogenase and implications for metabolic channeling in the shikimate pathway." Biochemistry 45(25);7787-96. PMID: 16784230
Singh07: Singh, S.A., Christendat, D. (2007). "The DHQ-dehydroshikimate-SDH-shikimate-NADP(H) Complex: Insights into Metabolite Transfer in the Shikimate Pathway." Crystal Growth and Design. 7(11):2153-2160.
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