EC |
1.1.1.24 |
Accepted name: |
quinate/shikimate dehydrogenase (NAD+) |
Reaction: |
L-quinate + NAD+ = 3-dehydroquinate + NADH + H+ |
|
For diagram of shikimate and chorismate biosynthesis, click here |
Glossary: |
quinate = (1R,3R,4R,5R)-1,3,4,5-tetrahydroxycyclohexanecarboxylic acid and is a cyclitol carboxylate
The numbering system used for the 3-dehydroquinate is that of the recommendations on cyclitols, sections I-8 and I-9: and is shown in the reaction diagram. The use of the term '5-dehydroquinate' for this compound is based on an earlier system of numbering. |
Other name(s): |
quinate dehydrogenase (ambiguous); quinic dehydrogenase (ambiguous); quinate:NAD oxidoreductase; quinate 5-dehydrogenase (ambiguous); quinate:NAD+ 5-oxidoreductase |
Systematic name: |
L-quinate:NAD+ 3-oxidoreductase |
Comments: |
The enzyme, found mostly in bacteria (mostly, but not exclusively in Gram-positive bacteria), fungi, and plants, participates in the degradation of quinate and shikimate with a strong preference for NAD+ as a cofactor. While the enzyme can act on both quinate and shikimate, activity is higher with the former. cf. EC 1.1.5.8, quinate/shikimate dehydrogenase (quinone), EC 1.1.1.282, quinate/shikimate dehydrogenase [NAD(P)+], and EC 1.1.1.25, shikimate dehydrogenase (NADP+). |
Links to other databases: |
BRENDA, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9028-28-8 |
References: |
1. |
Mitsuhashi, S. and Davis, B.D. Aromatic biosynthesis. XIII. Conversion of quinic acid to 5-dehydroquinic acid by quinic dehydrogenase. Biochim. Biophys. Acta 15 (1954) 268–280. [DOI] [PMID: 13208693] |
2. |
Gamborg, O.L. Aromatic metabolism in plants. III. Quinate dehydrogenase from mung bean cell suspension cultures. Biochim. Biophys. Acta 128 (1966) 483–491. |
3. |
Hawkins, A.R., Giles, N.H. and Kinghorn, J.R. Genetical and biochemical aspects of quinate breakdown in the filamentous fungus Aspergillus nidulans. Biochem. Genet. 20 (1982) 271–286. [PMID: 7049157] |
4. |
Singh, S., Stavrinides, J., Christendat, D. and Guttman, D.S. A phylogenomic analysis of the shikimate dehydrogenases reveals broadscale functional diversification and identifies one functionally distinct subclass. Mol. Biol. Evol. 25 (2008) 2221–2232. [DOI] [PMID: 18669580] |
5. |
Teramoto, H., Inui, M. and Yukawa, H. Regulation of expression of genes involved in quinate and shikimate utilization in Corynebacterium glutamicum. Appl. Environ. Microbiol. 75 (2009) 3461–3468. [DOI] [PMID: 19376919] |
6. |
Kubota, T., Tanaka, Y., Hiraga, K., Inui, M. and Yukawa, H. Characterization of shikimate dehydrogenase homologues of Corynebacterium glutamicum. Appl. Microbiol. Biotechnol. 97 (2013) 8139–8149. [DOI] [PMID: 23306642] |
7. |
Peek, J. and Christendat, D. The shikimate dehydrogenase family: functional diversity within a conserved structural and mechanistic framework. Arch. Biochem. Biophys. 566 (2015) 85–99. [DOI] [PMID: 25524738] |
|
[EC 1.1.1.24 created 1961, modified 1976, modified 2004, modified 2021] |
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|
|
|
EC |
1.1.1.25 |
Accepted name: |
shikimate dehydrogenase (NADP+) |
Reaction: |
shikimate + NADP+ = 3-dehydroshikimate + NADPH + H+ |
|
For diagram of shikimate and chorismate biosynthesis, click here |
Other name(s): |
shikimate dehydrogenase; dehydroshikimic reductase; shikimate oxidoreductase; shikimate:NADP+ oxidoreductase; 5-dehydroshikimate reductase; shikimate 5-dehydrogenase; 5-dehydroshikimic reductase; DHS reductase; shikimate:NADP+ 5-oxidoreductase; AroE |
Systematic name: |
shikimate:NADP+ 3-oxidoreductase |
Comments: |
NAD+ cannot replace NADP+ [3]. In higher organisms, this enzyme forms part of a multienzyme complex with EC 4.2.1.10, 3-dehydroquinate dehydratase [4]. cf. EC 1.1.1.24, quinate/shikimate dehydrogenase (NAD+), EC 1.1.5.8, quinate/shikimate dehydrogenase (quinone), and EC 1.1.1.282, quinate/shikimate dehydrogenase [NAD(P)+]. |
Links to other databases: |
BRENDA, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9026-87-3 |
References: |
1. |
Mitsuhashi, S. and Davis, B.D. Aromatic biosynthesis. XIII. Conversion of quinic acid to 5-dehydroquinic acid by quinic dehydrogenase. Biochim. Biophys. Acta 15 (1954) 268–280. [DOI] [PMID: 13208693] |
2. |
Yaniv, H. and Gilvarg, C. Aromatic biosynthesis. XIV. 5-Dehydroshikimic reductase. J. Biol. Chem. 213 (1955) 787–795. [PMID: 14367339] |
3. |
Balinsky, D. and Davies, D.D. Aromatic biosynthesis in higher plants. 1. Preparation and properties of dehydroshikimic reductase. Biochem. J. 80 (1961) 292–296. [PMID: 13686342] |
4. |
Chaudhuri, S. and Coggins, J.R. The purification of shikimate dehydrogenase from Escherichia coli. Biochem. J. 226 (1985) 217–223. [PMID: 3883995] |
5. |
Anton, I.A. and Coggins, J.R. Sequencing and overexpression of the Escherichia coli aroE gene encoding shikimate dehydrogenase. Biochem. J. 249 (1988) 319–326. [PMID: 3277621] |
6. |
Ye, S., Von Delft, F., Brooun, A., Knuth, M.W., Swanson, R.V. and McRee, D.E. The crystal structure of shikimate dehydrogenase (AroE) reveals a unique NADPH binding mode. J. Bacteriol. 185 (2003) 4144–4151. [DOI] [PMID: 12837789] |
|
[EC 1.1.1.25 created 1961, modified 1976, modified 2004, modified 2021] |
|
|
|
|
EC |
1.1.1.166 |
Accepted name: |
hydroxycyclohexanecarboxylate dehydrogenase |
Reaction: |
(1S,3R,4S)-3,4-dihydroxycyclohexane-1-carboxylate + NAD+ = (1S,4S)-4-hydroxy-3-oxocyclohexane-1-carboxylate + NADH + H+ |
Other name(s): |
dihydroxycyclohexanecarboxylate dehydrogenase; (-)t-3,t-4-dihydroxycyclohexane-c-1-carboxylate-NAD+ oxidoreductase |
Systematic name: |
(1S,3R,4S)-3,4-dihydroxycyclohexane-1-carboxylate:NAD+ 3-oxidoreductase |
Comments: |
Acts on hydroxycyclohexanecarboxylates that have an equatorial carboxy group at C-1, an axial hydroxy group at C-3 and an equatorial hydroxy or carbonyl group at C-4, including (-)-quinate and (-)-shikimate. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 55467-53-3 |
References: |
1. |
Whiting, G.C. and Coggins, R.A. A new nicotinamide-adenine dinucleotide-dependent hydroaromatic dehydrogenase of Lactobacillus plantarum and its role in formation of (-)t-3,t-4-dihydroxycyclohexane-c-1-carboxylate. Biochem. J. 141 (1974) 35–42. [PMID: 4375976] |
|
[EC 1.1.1.166 created 1976] |
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|
|
|
EC |
1.1.1.282 |
Accepted name: |
quinate/shikimate dehydrogenase [NAD(P)+] |
Reaction: |
(1) L-quinate + NAD(P)+ = 3-dehydroquinate + NAD(P)H + H+ (2) shikimate + NAD(P)+ = 3-dehydroshikimate + NAD(P)H + H+ |
|
For diagram of shikimate and chorismate biosynthesis, click here |
Glossary: |
quinate = (1R,3R,4R,5R)-1,3,4,5-tetrahydroxycyclohexanecarboxylic acid and is a cyclitol carboxylate
The numbering system used for the 3-dehydroquinate is that of the recommendations on cyclitols, sections I-8 and I-9: and is shown in the reaction diagram. The use of the term '5-dehydroquinate' for this compound is based on an earlier system of numbering. |
Other name(s): |
YdiB; quinate/shikimate dehydrogenase (ambiguous) |
Systematic name: |
L-quinate:NAD(P)+ 3-oxidoreductase |
Comments: |
This is the second shikimate dehydrogenase enzyme found in Escherichia coli. It can use both quinate and shikimate as substrates and either NAD+ or NADP+ as acceptor. The low catalytic efficiency with both quinate and shikimate suggests that neither may be the physiological substrate. cf. EC 1.1.1.24, quinate/shikimate dehydrogenase (NAD+), EC 1.1.5.8, quinate/shikimate dehydrogenase (quinone), and EC 1.1.1.25, shikimate dehydrogenase (NADP+). |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Michel, G., Roszak, A.W., Sauvé, V., Maclean, J., Matte, A., Coggins, J.R., Cygler, M. and Lapthorn, A.J. Structures of shikimate dehydrogenase AroE and its paralog YdiB. A common structural framework for different activities. J. Biol. Chem. 278 (2003) 19463–19472. [DOI] [PMID: 12637497] |
2. |
Benach, J., Lee, I., Edstrom, W., Kuzin, A.P., Chiang, Y., Acton, T.B., Montelione, G.T. and Hunt, J.F. The 2.3-Å crystal structure of the shikimate 5-dehydrogenase orthologue YdiB from Escherichia coli suggests a novel catalytic environment for an NAD-dependent dehydrogenase. J. Biol. Chem. 278 (2003) 19176–19182. [DOI] [PMID: 12624088] |
|
[EC 1.1.1.282 created 2004, modified 2021] |
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|
|
|
EC |
1.1.5.8 |
Accepted name: |
quinate/shikimate dehydrogenase (quinone) |
Reaction: |
quinate + quinone = 3-dehydroquinate + quinol |
|
For diagram of shikimate and chorismate biosynthesis, click here |
Glossary: |
quinate = (1R,3R,4R,5R)-1,3,4,5-tetrahydroxycyclohexanecarboxylic acid and is a cyclitol carboxylate
The numbering system used for the 3-dehydroquinate is that of the recommendations on cyclitols, sections I-8 and I-9: and is shown in the reaction diagram. The use of the term '5-dehydroquinate' for this compound is based on an earlier system of numbering. |
Other name(s): |
NAD(P)+-independent quinate dehydrogenase; quinate:pyrroloquinoline-quinone 5-oxidoreductase; quinate dehydrogenase (quinone) |
Systematic name: |
quinate:quinol 3-oxidoreductase |
Comments: |
The enzyme is membrane-bound. Does not use NAD(P)+ as acceptor. Contains pyrroloquinoline-quinone. cf. EC 1.1.1.24, quinate/shikimate dehydrogenase (NAD+), EC 1.1.1.282, quinate/shikimate dehydrogenase [NAD(P)+], and EC 1.1.1.25, shikimate dehydrogenase (NADP+). |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 115299-99-5 |
References: |
1. |
van Kleef, M.A.G. and Duine, J.A. Bacterial NAD(P)-independent quinate dehydrogenase is a quinoprotein. Arch. Microbiol. 150 (1988) 32–36. [PMID: 3044290] |
2. |
Adachi, O., Tanasupawat, S., Yoshihara, N., Toyama, H. and Matsushita, K. 3-Dehydroquinate production by oxidative fermentation and further conversion of 3-dehydroquinate to the intermediates in the shikimate pathway. Biosci. Biotechnol. Biochem. 67 (2003) 2124–2131. [DOI] [PMID: 14586099] |
3. |
Vangnai, A.S., Toyama, H., De-Eknamkul, W., Yoshihara, N., Adachi, O. and Matsushita, K. Quinate oxidation in Gluconobacter oxydans IFO3244: purification and characterization of quinoprotein quinate dehydrogenase. FEMS Microbiol. Lett. 241 (2004) 157–162. [DOI] [PMID: 15598527] |
|
[EC 1.1.5.8 created 1992 as EC 1.1.99.25, modified 2004, transferred 2010 to EC 1.1.5.8, modified 2021] |
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|
|
|
EC
|
1.1.99.25
|
Transferred entry: | quinate dehydrogenase (pyrroloquinoline-quinone). Now EC 1.1.5.8, quinate dehydrogenase (quinone)
|
[EC 1.1.99.25 created 1992, modified 2004, deleted 2010] |
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|
|
|
EC |
1.4.1.24 |
Accepted name: |
3-dehydroquinate synthase II |
Reaction: |
2-amino-3,7-dideoxy-D-threo-hept-6-ulosonate + H2O + NAD+ = 3-dehydroquinate + NH3 + NADH + H+ |
|
For diagram of 3-dehydroquinate biosynthesis in archaea, click here |
Glossary: |
2-amino-3,7-dideoxy-D-threo-hept-6-ulosonate = 2-amino-2,3,7-trideoxy-D-lyxo-hept-6-ulosonate |
Other name(s): |
DHQ synthase II; MJ1249 (gene name); aroB′ (gene name) |
Systematic name: |
2-amino-3,7-dideoxy-D-threo-hept-6-ulosonate:NAD+ oxidoreductase (deaminating) |
Comments: |
The enzyme, which was isolated from the archaeon Methanocaldococcus jannaschii, plays a key role in an alternative pathway for the biosynthesis of 3-dehydroquinate (DHQ), an intermediate of the canonical pathway for the biosynthesis of aromatic amino acids. The enzyme catalyses a two-step reaction - an oxidative deamination, followed by cyclization. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
White, R.H. L-Aspartate semialdehyde and a 6-deoxy-5-ketohexose 1-phosphate are the precursors to the aromatic amino acids in Methanocaldococcus jannaschii. Biochemistry 43 (2004) 7618–7627. [DOI] [PMID: 15182204] |
|
[EC 1.4.1.24 created 2012] |
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|
|
EC
|
1.14.13.36
|
Transferred entry: | 5-O-(4-coumaroyl)-D-quinate 3′-monooxygenase. Now EC 1.14.14.96, 5-O-(4-coumaroyl)-D-quinate 3′-monooxygenase
|
[EC 1.14.13.36 created 1990, deleted 2018] |
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|
|
|
EC |
1.14.14.96 |
Accepted name: |
5-O-(4-coumaroyl)-D-quinate 3′-monooxygenase |
Reaction: |
trans-5-O-(4-coumaroyl)-D-quinate + [reduced NADPH—hemoprotein reductase] + O2 = trans-5-O-caffeoyl-D-quinate + [oxidized NADPH—hemoprotein reductase] + H2O |
Other name(s): |
5-O-(4-coumaroyl)-D-quinate/shikimate 3′-hydroxylase; coumaroylquinate(coumaroylshikimate) 3′-monooxygenase; CYP98A3 (gene name) |
Systematic name: |
trans-5-O-(4-coumaroyl)-D-quinate,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (3′-hydroxylating) |
Comments: |
A cytochrome P-450 (heme-thiolate) protein, found in plants. It also acts on trans-5-O-(4-coumaroyl)shikimate. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 112131-08-5 |
References: |
1. |
Kühnl, T., Koch, U., Heller, W. and Wellman, E. Chlorogenic acid biosynthesis: characterization of a light-induced microsomal 5-O-(4-coumaroyl)-D-quinate/shikimate 3′-hydroxylase from carrot (Daucus carota L.) cell suspension cultures. Arch. Biochem. Biophys. 258 (1987) 226–232. [DOI] [PMID: 2821918] |
2. |
Schoch, G., Goepfert, S., Morant, M., Hehn, A., Meyer, D., Ullmann, P. and Werck-Reichhart, D. CYP98A3 from Arabidopsis thaliana is a 3′-hydroxylase of phenolic esters, a missing link in the phenylpropanoid pathway. J. Biol. Chem. 276 (2001) 36566–36574. [PMID: 11429408] |
3. |
Franke, R., Humphreys, J.M., Hemm, M.R., Denault, J.W., Ruegger, M.O., Cusumano, J.C. and Chapple, C. The Arabidopsis REF8 gene encodes the 3-hydroxylase of phenylpropanoid metabolism. Plant J. 30 (2002) 33–45. [PMID: 11967091] |
4. |
Matsuno, M., Compagnon, V., Schoch, G.A., Schmitt, M., Debayle, D., Bassard, J.E., Pollet, B., Hehn, A., Heintz, D., Ullmann, P., Lapierre, C., Bernier, F., Ehlting, J. and Werck-Reichhart, D. Evolution of a novel phenolic pathway for pollen development. Science 325 (2009) 1688–1692. [PMID: 19779199] |
|
[EC 1.14.14.96 created 1990 as EC 1.14.13.36, transferred 2018 to EC 1.14.14.96] |
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|
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|
EC |
2.2.1.10 |
Accepted name: |
2-amino-3,7-dideoxy-D-threo-hept-6-ulosonate synthase |
Reaction: |
L-aspartate 4-semialdehyde + 1-deoxy-D-threo-hexo-2,5-diulose 6-phosphate = 2-amino-3,7-dideoxy-D-threo-hept-6-ulosonate + 2,3-dioxopropyl phosphate |
|
For diagram of 3-dehydroquinate biosynthesis in archaea, click here |
Glossary: |
1-deoxy-D-threo-hexo-2,5-diulose 6-phosphate = 6-deoxy-5-ketofructose 1-phosphate
2-amino-3,7-dideoxy-D-threo-hept-6-ulosonate = 2-amino-2,3,7-trideoxy-D-lyxo-hept-6-ulosonate
|
Other name(s): |
ADH synthase; ADHS; MJ0400 (gene name) |
Systematic name: |
L-aspartate 4-semialdehyde:1-deoxy-D-threo-hexo-2,5-diulose 6-phosphate methylglyoxaltransferase |
Comments: |
The enzyme plays a key role in an alternative pathway of the biosynthesis of 3-dehydroquinate (DHQ), which is involved in the canonical pathway for the biosynthesis of aromatic amino acids. The enzyme can also catalyse the reaction of EC 4.1.2.13, fructose-bisphosphate aldolase. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
White, R.H. L-Aspartate semialdehyde and a 6-deoxy-5-ketohexose 1-phosphate are the precursors to the aromatic amino acids in Methanocaldococcus jannaschii. Biochemistry 43 (2004) 7618–7627. [DOI] [PMID: 15182204] |
2. |
Samland, A.K., Wang, M. and Sprenger, G.A. MJ0400 from Methanocaldococcus jannaschii exhibits fructose-1,6-bisphosphate aldolase activity. FEMS Microbiol. Lett. 281 (2008) 36–41. [DOI] [PMID: 18318840] |
3. |
Morar, M., White, R.H. and Ealick, S.E. Structure of 2-amino-3,7-dideoxy-D-threo-hept-6-ulosonic acid synthase, a catalyst in the archaeal pathway for the biosynthesis of aromatic amino acids. Biochemistry 46 (2007) 10562–10571. [DOI] [PMID: 17713928] |
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[EC 2.2.1.10 created 2012] |
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|
|
EC |
2.2.1.11 |
Accepted name: |
6-deoxy-5-ketofructose 1-phosphate synthase |
Reaction: |
(1) 2-oxopropanal + D-fructose 1,6-bisphosphate = D-glyceraldehyde 3-phosphate + 1-deoxy-D-threo-hexo-2,5-diulose 6-phosphate (2) 2-oxopropanal + D-fructose 1-phosphate = D-glyceraldehyde + 1-deoxy-D-threo-hexo-2,5-diulose 6-phosphate |
|
For diagram of 3-dehydroquinate biosynthesis in archaea, click here |
Glossary: |
2-oxopropanal = methylglyoxal
1-deoxy-D-threo-hexo-2,5-diulose 6-phosphate = 6-deoxy-5-ketofructose 1-phosphate |
Other name(s): |
DKFP synthase |
Systematic name: |
2-oxopropanal:D-fructose 1,6-bisphosphate glycerone-phosphotransferase |
Comments: |
The enzyme plays a key role in an alternative pathway of the biosynthesis of 3-dehydroquinate (DHQ), which is involved in the canonical pathway for the biosynthesis of aromatic amino acids. The enzyme can also catalyse the reaction of EC 4.1.2.13, fructose-bisphosphate aldolase. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
White, R.H. and Xu, H. Methylglyoxal is an intermediate in the biosynthesis of 6-deoxy-5-ketofructose-1-phosphate: a precursor for aromatic amino acid biosynthesis in Methanocaldococcus jannaschii. Biochemistry 45 (2006) 12366–12379. [DOI] [PMID: 17014089] |
2. |
Samland, A.K., Wang, M. and Sprenger, G.A. MJ0400 from Methanocaldococcus jannaschii exhibits fructose-1,6-bisphosphate aldolase activity. FEMS Microbiol. Lett. 281 (2008) 36–41. [DOI] [PMID: 18318840] |
|
[EC 2.2.1.11 created 2012] |
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EC |
2.3.1.98 |
Accepted name: |
chlorogenate—glucarate O-hydroxycinnamoyltransferase |
Reaction: |
chlorogenate + glucarate = quinate + 2-O-caffeoylglucarate |
Other name(s): |
chlorogenate:glucarate caffeoyltransferase; chlorogenic acid:glucaric acid O-caffeoyltransferase; chlorogenate:glucarate caffeoyltransferase |
Systematic name: |
chlorogenate:glucarate O-(hydroxycinnamoyl)transferase |
Comments: |
Galactarate can act as acceptor, more slowly. Involved with EC 2.3.1.99 quinate O-hydroxycinnamoyltransferase in the formation of caffeoylglucarate in tomato. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 126124-92-3 |
References: |
1. |
Strack, D. and Gross, W. Properties and activity changes of chlorogenic acid - glucaric acid caffeoyltransferase from tomato (Lycopersicon esculentum). Plant Physiol. 92 (1990) 41–47. [PMID: 16667263] |
2. |
Strack, D., Gross, W., Wray, V. and Grotjahn, L. Enzymatic-synthesis of caffeoylglucaric acid from chlorogenic acid and glucaric acid by a protein preparation from tomato cotyledons. Plant Physiol. 83 (1987) 475–478. [PMID: 16665274] |
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[EC 2.3.1.98 created 1989, modified 1990] |
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|
EC |
2.3.1.99 |
Accepted name: |
quinate O-hydroxycinnamoyltransferase |
Reaction: |
feruloyl-CoA + quinate = CoA + O-feruloylquinate |
Other name(s): |
hydroxycinnamoyl coenzyme A-quinate transferase |
Systematic name: |
feruloyl-CoA:quinate O-(hydroxycinnamoyl)transferase |
Comments: |
Caffeoyl-CoA and 4-coumaroyl-CoA can also act as donors, but more slowly. Involved in the biosynthesis of chlorogenic acid in sweet potato and, with EC 2.3.1.98 chlorogenate—glucarate O-hydroxycinnamoyltransferase, in the formation of caffeoyl-CoA in tomato. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 60321-02-0 |
References: |
1. |
Strack, D., Gross, W., Wray, V. and Grotjahn, L. Enzymatic-synthesis of caffeoylglucaric acid from chlorogenic acid and glucaric acid by a protein preparation from tomato cotyledons. Plant Physiol. 83 (1987) 475–478. [PMID: 16665274] |
2. |
Strack, D., Keller, H. and Weissenböck, G. Enzymatic-synthesis of hydroxycinnamic acid-esters of sugar acids and hydroaromatic acids by protein preparations from rye (Secale cereale) primary leaves. J. Plant Physiol. 131 (1987) 61–73. |
3. |
Villegas, R.J.A. and Kojima, M. Purification and characterization of hydroxycinnamoyl D-glucose. Quinate hydroxycinnamoyl transferase in the root of sweet potato, Ipomoea batatas Lam. J. Biol. Chem. 261 (1986) 8729–8733. [PMID: 3722170] |
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[EC 2.3.1.99 created 1989, modified 1990] |
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|
|
EC |
3.1.1.42 |
Accepted name: |
chlorogenate hydrolase |
Reaction: |
chlorogenate + H2O = caffeate + quinate |
Other name(s): |
chlorogenase; chlorogenic acid esterase |
Systematic name: |
chlorogenate hydrolase |
Comments: |
Also acts, more slowly, on isochlorogenate. No other substrates are known. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 74082-59-0 |
References: |
1. |
Schöbel, B. and Pollmann, W. Isolation and characterization of a chlorogenic acid esterase from Aspergillus niger. Z. Naturforsch. C: Biosci. 35 (1980) 209–212. [PMID: 7385941] |
2. |
Schöbel, B. and Pollmann, W. Weitere Charakterisierung einer Chlorogensäure - Hydrolase aus Aspergillus niger. Z. Naturforsch. C: Biosci. 35 (1980) 699–701. [PMID: 7445677] |
|
[EC 3.1.1.42 created 1981] |
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|
|
EC |
4.2.1.10 |
Accepted name: |
3-dehydroquinate dehydratase |
Reaction: |
3-dehydroquinate = 3-dehydroshikimate + H2O |
|
For diagram of shikimate and chorismate biosynthesis, click here and for mechanism of reaction, click here |
Glossary: |
quinate = (1R,3R,4R,5R)-1,3,4,5-tetrahydroxycyclohexanecarboxylic acid and is a cyclitol carboxylate
The numbering system used for the 3-dehydroquinate is that of the recommendations on cyclitols, sections I-8 and I-9: and is shown in the reaction diagram). The use of the term ’5-dehydroquinate’ for this compound is based on an earlier system of numbering. |
Other name(s): |
3-dehydroquinate hydrolase; DHQase; dehydroquinate dehydratase; 3-dehydroquinase; 5-dehydroquinase; dehydroquinase; 5-dehydroquinate dehydratase; 5-dehydroquinate hydro-lyase; 3-dehydroquinate hydro-lyase |
Systematic name: |
3-dehydroquinate hydro-lyase (3-dehydroshikimate-forming) |
Links to other databases: |
BRENDA, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9012-66-2 |
References: |
1. |
Mitsuhashi, S. and Davis, B.D. Aromatic biosynthesis. XII. Conversion of 5-dehydroquinic acid to 5-dehydroshikimic acid by 5-dehydroquinase. Biochim. Biophys. Acta 15 (1954) 54–61. [DOI] [PMID: 13198937] |
2. |
Mitsuhashi, S. and Davis, B.D. Aromatic biosynthesis. XIII. Conversion of quinic acid to 5-dehydroquinic acid by quinic dehydrogenase. Biochim. Biophys. Acta 15 (1954) 268–280. [DOI] [PMID: 13208693] |
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[EC 4.2.1.10 created 1961, modified 1976] |
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EC |
4.2.3.4 |
Accepted name: |
3-dehydroquinate synthase |
Reaction: |
3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate = 3-dehydroquinate + phosphate |
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For diagram of shikimate and chorismate biosynthesis, click here and for mechanism of reaction, click here |
Glossary: |
quinate = (1R,3R,4R,5R)-1,3,4,5-tetrahydroxycyclohexanecarboxylic acid and is a cyclitol carboxylate The numbering system used for the 3-dehydroquinate is that of the recommendations on cyclitols, sections I-8 and I-9: and is shown in the reaction diagram). The use of the term ’5-dehydroquinate’ for this compound is based on an earlier system of numbering. |
Other name(s): |
5-dehydroquinate synthase; 5-dehydroquinic acid synthetase; dehydroquinate synthase; 3-dehydroquinate synthetase; 3-deoxy-arabino-heptulosonate-7-phosphate phosphate-lyase (cyclizing); 3-deoxy-arabino-heptulonate-7-phosphate phosphate-lyase (cyclizing); 3-deoxy-arabino-heptulonate-7-phosphate phosphate-lyase (cyclizing; 3-dehydroquinate-forming) |
Systematic name: |
3-deoxy-D-arabino-hept-2-ulosonate-7-phosphate phosphate-lyase (cyclizing; 3-dehydroquinate-forming) |
Comments: |
Requires Co2+ and bound NAD+. The hydrogen atoms on C-7 of the substrate are retained on C-2 of the product. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37211-77-1 |
References: |
1. |
Rotenberg, S.L. and Sprinson, D.B. Mechanism and stereochemistry of 5-dehydroquinate synthetase. Proc. Natl. Acad. Sci. USA 67 (1970) 1669–1672. [DOI] [PMID: 5275368] |
2. |
Srinivasan, P.R., Rothschild, J. and Sprinson, D.B. The enzymic conversion of 3-deoxy-D-arabino-heptulosonic acid 7-phosphate to 5-dehydroquinate. J. Biol. Chem. 238 (1963) 3176–3182. [PMID: 14085358] |
3. |
Bender, S.L., Mehdi, S. and Knowles, J.R. Dehydroquinate synthase: the role of divalent metal cations and of nicotinamide adenine dinucleotide in catalysis. Biochemistry 28 (1989) 7555–7560. [PMID: 2514789] |
4. |
Carpenter, E.P., Hawkins, A.R., Frost, J.W. and Brown, K.A. Structure of dehydroquinate synthase reveals an active site capable of multistep catalysis. Nature 394 (1998) 299–302. [DOI] [PMID: 9685163] |
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[EC 4.2.3.4 created 1978 as EC 4.6.1.3, transferred 2000 to EC 4.2.3.4, modified 2002] |
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EC |
4.2.3.124 |
Accepted name: |
2-deoxy-scyllo-inosose synthase |
Reaction: |
D-glucose 6-phosphate = 2-deoxy-L-scyllo-inosose + phosphate |
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For diagram of paromamine biosynthesis, click here |
Other name(s): |
btrC (gene name); neoC (gene name); kanC (gene name) |
Systematic name: |
D-glucose-6-phosphate phosphate-lyase (2-deoxy-L-scyllo-inosose-forming) |
Comments: |
Requires Co2+ [2]. Involved in the biosynthetic pathways of several clinically important aminocyclitol antibiotics, including kanamycin, butirosin, neomycin and ribostamycin. Requires an NAD+ cofactor, which is transiently reduced during the reaction [1,4]. The enzyme from the bacterium Bacillus circulans forms a complex with the glutamine amidotransferase subunit of pyridoxal 5′-phosphate synthase (EC 4.3.3.6), which appears to stabilize the complex [6,7]. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Kudo, F., Yamauchi, N., Suzuki, R. and Kakinuma, K. Kinetic isotope effect and reaction mechanism of 2-deoxy-scyllo-inosose synthase derived from butirosin-producing Bacillus circulans. J. Antibiot. (Tokyo) 50 (1997) 424–428. [PMID: 9207913] |
2. |
Kudo, F., Hosomi, Y., Tamegai, H. and Kakinuma, K. Purification and characterization of 2-deoxy-scyllo-inosose synthase derived from Bacillus circulans. A crucial carbocyclization enzyme in the biosynthesis of 2-deoxystreptamine-containing aminoglycoside antibiotics. J. Antibiot. (Tokyo) 52 (1999) 81–88. [PMID: 10344560] |
3. |
Kudo, F., Tamegai, H., Fujiwara, T., Tagami, U., Hirayama, K. and Kakinuma, K. Molecular cloning of the gene for the key carbocycle-forming enzyme in the biosynthesis of 2-deoxystreptamine-containing aminocyclitol antibiotics and its comparison with dehydroquinate synthase. J. Antibiot. (Tokyo) 52 (1999) 559–571. [PMID: 10470681] |
4. |
Huang, Z., Kakinuma, K. and Eguchi, T. Stereospecificity of hydride transfer in NAD+-catalyzed 2-deoxy-scyllo-inosose synthase, the key enzyme in the biosynthesis of 2-deoxystreptamine-containing aminocyclitol antibiotics. Bioorg. Chem. 33 (2005) 82–89. [DOI] [PMID: 15788164] |
5. |
Thuy, M.L., Kharel, M.K., Lamichhane, R., Lee, H.C., Suh, J.W., Liou, K. and Sohng, J.K. Expression of 2-deoxy-scyllo-inosose synthase (kanA) from kanamycin gene cluster in Streptomyces lividans. Biotechnol. Lett. 27 (2005) 465–470. [DOI] [PMID: 15928851] |
6. |
Tamegai, H., Nango, E., Koike-Takeshita, A., Kudo, F. and Kakinuma, K. Significance of the 20-kDa subunit of heterodimeric 2-deoxy-scyllo-inosose synthase for the biosynthesis of butirosin antibiotics in Bacillus circulans. Biosci. Biotechnol. Biochem. 66 (2002) 1538–1545. [PMID: 12224638] |
7. |
Tamegai, H., Sawada, H., Nango, E., Aoki, R., Hirakawa, H., Iino, T. and Eguchi, T. Roles of a 20 kDa protein associated with a carbocycle-forming enzyme involved in aminoglycoside biosynthesis in primary and secondary metabolism. Biosci. Biotechnol. Biochem. 74 (2010) 1215–1219. [DOI] [PMID: 20530911] |
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[EC 4.2.3.124 created 2012] |
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EC |
4.2.3.152 |
Accepted name: |
2-epi-5-epi-valiolone synthase |
Reaction: |
α-D-sedoheptulopyranose 7-phosphate = 2-epi-5-epi-valiolone + phosphate |
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For diagram of valiolone biosynthesis, click here |
Glossary: |
2-epi-5-epi-valiolone = (2S,3S,4S,5R)-2,3,4,5-tetrahydroxy-5-(hydroxymethyl)cyclohexan-1-one |
Other name(s): |
AcbC; ValA; CetA; SalQ; C7-cyclitol synthase |
Systematic name: |
α-D-sedoheptulopyranose-7-phosphate phosphate-lyase (cyclizing; 2-epi-5-epi-valiolone-forming) |
Comments: |
The enzyme is highly specific for α-D-sedoheptulopyranose 7-phosphate. It requires a divalent metal ion (Zn2+ or Co2+) and an NAD+ cofactor, which is transiently reduced during the reaction. The enzyme is involved in the biosynthesis of C7N-aminocyclitol natural products, such as the valienamine moiety of the antidiabetic drug acarbose and the crop protectant validamycin A. cf. EC 4.2.3.155, 2-epi-valiolone synthase and EC 4.2.3.154, demethyl-4-deoxygadusol synthase. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Stratmann, A., Mahmud, T., Lee, S., Distler, J., Floss, H.G. and Piepersberg, W. The AcbC protein from Actinoplanes species is a C7-cyclitol synthase related to 3-dehydroquinate synthases and is involved in the biosynthesis of the α-glucosidase inhibitor acarbose. J. Biol. Chem. 274 (1999) 10889–10896. [DOI] [PMID: 10196166] |
2. |
Yu, Y., Bai, L., Minagawa, K., Jian, X., Li, L., Li, J., Chen, S., Cao, E., Mahmud, T., Floss, H.G., Zhou, X. and Deng, Z. Gene cluster responsible for validamycin biosynthesis in Streptomyces hygroscopicus subsp. jinggangensis 5008. Appl. Environ. Microbiol. 71 (2005) 5066–5076. [DOI] [PMID: 16151088] |
3. |
Wu, X., Flatt, P.M., Schlorke, O., Zeeck, A., Dairi, T. and Mahmud, T. A comparative analysis of the sugar phosphate cyclase superfamily involved in primary and secondary metabolism. ChemBioChem 8 (2007) 239–248. [DOI] [PMID: 17195255] |
4. |
Choi, W.S., Wu, X., Choeng, Y.H., Mahmud, T., Jeong, B.C., Lee, S.H., Chang, Y.K., Kim, C.J. and Hong, S.K. Genetic organization of the putative salbostatin biosynthetic gene cluster including the 2-epi-5-epi-valiolone synthase gene in Streptomyces albus ATCC 21838. Appl. Microbiol. Biotechnol. 80 (2008) 637–645. [DOI] [PMID: 18648803] |
5. |
Kean, K.M., Codding, S.J., Asamizu, S., Mahmud, T. and Karplus, P.A. Structure of a sedoheptulose 7-phosphate cyclase: ValA from Streptomyces hygroscopicus. Biochemistry 53 (2014) 4250–4260. [DOI] [PMID: 24832673] |
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[EC 4.2.3.152 created 2015, modified 2016] |
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EC
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4.6.1.3
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Transferred entry: | 3-dehydroquinate synthase. Now EC 4.2.3.4, 3-dehydroquinate synthase
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[EC 4.6.1.3 created 1978, deleted 2000] |
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