The Enzyme Database

Your query returned 5 entries.    printer_iconPrintable version



EC 2.3.1.206     
Accepted name: 3,5,7-trioxododecanoyl-CoA synthase
Reaction: 3 malonyl-CoA + hexanoyl-CoA = 3 CoA + 3,5,7-trioxododecanoyl-CoA + 3 CO2
For diagram of cannabinoid biosynthesis, click here
Other name(s): TKS (ambiguous); olivetol synthase (incorrect)
Systematic name: malonyl-CoA:hexanoyl-CoA malonyltransferase (3,5,7-trioxododecanoyl-CoA-forming)
Comments: A polyketide synthase catalysing the first committed step in the cannabinoids biosynthetic pathway of the plant Cannabis sativa. The enzyme was previously thought to also function as a cyclase, but the cyclization is now known to be catalysed by EC 4.4.1.26, olivetolic acid cyclase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Taura, F., Tanaka, S., Taguchi, C., Fukamizu, T., Tanaka, H., Shoyama, Y. and Morimoto, S. Characterization of olivetol synthase, a polyketide synthase putatively involved in cannabinoid biosynthetic pathway. FEBS Lett. 583 (2009) 2061–2066. [DOI] [PMID: 19454282]
2.  Gagne, S.J., Stout, J.M., Liu, E., Boubakir, Z., Clark, S.M. and Page, J.E. Identification of olivetolic acid cyclase from Cannabis sativa reveals a unique catalytic route to plant polyketides. Proc. Natl. Acad. Sci. USA 109 (2012) 12811–12816. [DOI] [PMID: 22802619]
[EC 2.3.1.206 created 2012]
 
 
EC 2.3.1.301     
Accepted name: mycobacterial β-ketoacyl-[acyl carrier protein] synthase III
Reaction: dodecanoyl-CoA + a malonyl-[acyl-carrier protein] = a 3-oxotetradecanoyl-[acyl-carrier protein] + CoA + CO2
Glossary: dodecanoyl-CoA = lauroyl-CoA
Other name(s): fabH (gene name) (ambiguous); mycobacterial 3-oxoacyl-[acyl carrier protein] synthase III
Systematic name: dodecanoyl-CoA:malonyl-[acyl-carrier protein] C-acyltransferase
Comments: The enzyme, characterized from mycobacteria, provides a link between the type I and type II fatty acid synthase systems (FAS-I and FAS-II, respectively) found in these organisms. The enzyme acts on medium- and long-chain acyl-CoAs (C12-C16) produced by the FAS-I system, condensing them with malonyl-[acyl-carrier protein] (malonyl-AcpM) and forming starter molecules for the FAS-II system, which elongates them into meromycolic acids. The enzyme has no activity with short-chain acyl-CoAs (e.g. acetyl-CoA), which are used by EC 2.3.1.180, β-ketoacyl-[acyl-carrier-protein] synthase III, or branched-chain acyl-CoAs, which are used by EC 2.3.1.300, branched-chain β-ketoacyl-[acyl-carrier-protein] synthase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Scarsdale, J.N., Kazanina, G., He, X., Reynolds, K.A. and Wright, H.T. Crystal structure of the Mycobacterium tuberculosis β-ketoacyl-acyl carrier protein synthase III. J. Biol. Chem. 276 (2001) 20516–20522. [DOI] [PMID: 11278743]
2.  Musayev, F., Sachdeva, S., Scarsdale, J.N., Reynolds, K.A. and Wright, H.T. Crystal structure of a substrate complex of Mycobacterium tuberculosis β-ketoacyl-acyl carrier protein synthase III (FabH) with lauroyl-coenzyme A. J. Mol. Biol. 346 (2005) 1313–1321. [DOI] [PMID: 15713483]
3.  Brown, A.K., Sridharan, S., Kremer, L., Lindenberg, S., Dover, L.G., Sacchettini, J.C. and Besra, G.S. Probing the mechanism of the Mycobacterium tuberculosis β-ketoacyl-acyl carrier protein synthase III mtFabH: factors influencing catalysis and substrate specificity. J. Biol. Chem. 280 (2005) 32539–32547. [DOI] [PMID: 16040614]
4.  Sachdeva, S., Musayev, F.N., Alhamadsheh, M.M., Scarsdale, J.N., Wright, H.T. and Reynolds, K.A. Separate entrance and exit portals for ligand traffic in Mycobacterium tuberculosis FabH. Chem. Biol. 15 (2008) 402–412. [DOI] [PMID: 18420147]
[EC 2.3.1.301 created 2021]
 
 
EC 2.3.3.2     
Accepted name: decylcitrate synthase
Reaction: lauroyl-CoA + H2O + oxaloacetate = (2S,3S)-2-hydroxytridecane-1,2,3-tricarboxylate + CoA
For diagram of reaction, click here
Other name(s): 2-decylcitrate synthase; (2S,3S)-2-hydroxytridecane-1,2,3-tricarboxylate oxaloacetate-lyase (CoA-acylating)
Systematic name: dodecanoyl-CoA:oxaloacetate C-dodecanoyltransferase (thioester-hydrolysing, 1-carboxyundecyl-forming)
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9068-72-8
References:
1.  Maahlén, A. and Gatenbeck, S. A metabolic variation in Penicillium spiculisporum Lehman. II. Purification and some properties of the enzyme synthesizing (-)-decylcitric acid. Acta Chem. Scand. 22 (1968) 2617–2623. [PMID: 5719165]
2.  Maahlén, A. Properties of 2-decylcitrate synthase from Penicillium spiculisporum Lehman. Eur. J. Biochem. 22 (1971) 104–114. [DOI] [PMID: 5099208]
[EC 2.3.3.2 created 1972 as EC 4.1.3.23, transferred 2002 to EC 2.3.3.2]
 
 
EC 2.3.3.4     
Accepted name: decylhomocitrate synthase
Reaction: dodecanoyl-CoA + H2O + 2-oxoglutarate = (3S,4S)-3-hydroxytetradecane-1,3,4-tricarboxylate + CoA
For diagram of reaction, click here
Other name(s): 2-decylhomocitrate synthase; 3-hydroxytetradecane-1,3,4-tricarboxylate 2-oxoglutarate-lyase (CoA-acylating)
Systematic name: dodecanoyl-CoA:2-oxoglutarate C-dodecanoyltransferase (thioester-hydrolysing, 1-carboxyundecyl-forming)
Comments: Decanoyl-CoA can act instead of dodecanoyl-CoA, but 2-oxoglutarate cannot be replaced by oxaloacetate or pyruvate.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 51845-40-0
References:
1.  Maahlén, A. Purification and some properties of 2-decylhomocitrate synthase from Penicillium spiculisporum. Eur. J. Biochem. 38 (1973) 32–39. [DOI] [PMID: 4774124]
2.  Brandäge, S., Dahlman, O., Lindqvist, B., Maahlén, A. and Mörch, L. Absolute configuration and enantiospecific synthesis of spiculisporic acid. Acta Chem. Scand. 38B (1984) 837–844.
[EC 2.3.3.4 created 1976 as EC 4.1.3.29, transferred 2002 to EC 2.3.3.4]
 
 
EC 4.4.1.26     
Accepted name: olivetolic acid cyclase
Reaction: 3,5,7-trioxododecanoyl-CoA = CoA + 2,4-dihydroxy-6-pentylbenzoate
For diagram of cannabinoid biosynthesis, click here
Glossary: 2,4-dihydroxy-6-pentylbenzoate = olivetolate
Other name(s): OAC
Systematic name: 3,5,7-trioxododecanoyl-CoA CoA-lyase (2,4-dihydroxy-6-pentylbenzoate-forming)
Comments: Part of the cannabinoids biosynthetic pathway in the plant Cannabis sativa.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Gagne, S.J., Stout, J.M., Liu, E., Boubakir, Z., Clark, S.M. and Page, J.E. Identification of olivetolic acid cyclase from Cannabis sativa reveals a unique catalytic route to plant polyketides. Proc. Natl. Acad. Sci. USA 109 (2012) 12811–12816. [DOI] [PMID: 22802619]
[EC 4.4.1.26 created 2012]
 
 


Data © 2001–2022 IUBMB
Web site © 2005–2022 Andrew McDonald