The Enzyme Database

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EC 1.17.1.2      
Transferred entry: 4-hydroxy-3-methylbut-2-enyl diphosphate reductase, now classified as EC 1.17.7.4, 4-hydroxy-3-methylbut-2-enyl diphosphate reductase.
[EC 1.17.1.2 created 2003, modified 2009, deleted 2016]
 
 
EC 1.17.7.4     
Accepted name: 4-hydroxy-3-methylbut-2-en-1-yl diphosphate reductase
Reaction: (1) isopentenyl diphosphate + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O = (E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
(2) dimethylallyl diphosphate + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O = (E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
For diagram of non-mevalonate terpenoid biosynthesis, click here
Glossary: isopentenyl diphosphate = 3-methylbut-3-en-1-yl diphosphate
Other name(s): isopentenyl-diphosphate:NADP+ oxidoreductase; LytB; (E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate reductase; HMBPP reductase; IspH; LytB/IspH
Systematic name: isopentenyl-diphosphate:ferredoxin oxidoreductase
Comments: An iron-sulfur protein that contains either a [3Fe-4S] [6] or a [4Fe-4S] [5] cluster. This enzyme forms a system with a ferredoxin or a flavodoxin and an NAD(P)H-dependent reductase. This is the last enzyme in the non-mevalonate pathway for isoprenoid biosynthesis. This pathway, also known as the 1-deoxy-D-xylulose 5-phosphate (DOXP) or as the 2-C-methyl-D-erythritol-4-phosphate (MEP) pathway, is found in most bacteria and in plant chloroplasts. The enzyme acts in the reverse direction, producing a 5:1 mixture of isopentenyl diphosphate and dimethylallyl diphosphate.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 512789-14-9
References:
1.  Rohdich, F., Hecht, S., Gärtner, K., Adam, P., Krieger, C., Amslinger, S., Arigoni, D., Bacher, A. and Eisenreich, W. Studies on the nonmevalonate terpene biosynthetic pathway: Metabolic role of IspH (LytB) protein. Proc. Natl. Acad. Sci. USA 99 (2002) 1158–1163. [DOI] [PMID: 11818558]
2.  Hintz, M., Reichenberg, A., Altincicek, B., Bahr, U., Gschwind, R.M., Kollas, A.-K., Beck, E., Wiesner, J., Eberl, M. and Jomaa, H. Identification of (E)-4-hydroxy-3-methyl-but-2-enyl pyrophosphate as a major activator for human T cells in Escherichia coli. FEBS Lett. 509 (2001) 317–322. [DOI] [PMID: 11741609]
3.  Charon, L., Pale-Grosdemange, C. and Rohmer, M. On the reduction steps in the mevalonate independent 2-C-methyl-D-erythritol 4-phosphate (MEP) pathway for isoprenoid biosynthesis in the bacterium Zymomonas mobilis. Tetrahedron Lett. 40 (1999) 7231–7234.
4.  Röhrich, R.C., Englert, N., Troschke, K., Reichenberg, A., Hintz, M., Seeber, F., Balconi, E., Aliverti, A., Zanetti, G., Köhler, U., Pfeiffer, M., Beck, E., Jomaa, H. and Wiesner, J. Reconstitution of an apicoplast-localised electron transfer pathway involved in the isoprenoid biosynthesis of Plasmodium falciparum. FEBS Lett. 579 (2005) 6433–6438. [DOI] [PMID: 16289098]
5.  Wolff, M., Seemann, M., Bui, T.S.B., Frapart, Y., Tritsch, D., Garcia Estrabot, A., Rodríguez-Concepción, M., Boronat, A., Marquet, A. and Rohmer, M. Isoprenoid biosynthesis via the methylerythritol phosphate pathway: the (E)-4-hydroxy-3-methylbut-2-enyl diphosphate reductase (LytB/IspH) from Escherichia coli is a [4Fe-4S] protein. FEBS Lett. 541 (2003) 115–120. [DOI] [PMID: 12706830]
6.  Gräwert, T., Kaiser, J., Zepeck, F., Laupitz, R., Hecht, S., Amslinger, S., Schramek, N., Schleicher, E., Weber, S., Haslbeck, M., Buchner, J., Rieder, C., Arigoni, D., Bacher, A., Eisenreich, W. and Rohdich, F. IspH protein of Escherichia coli: studies on iron-sulfur cluster implementation and catalysis. J. Am. Chem. Soc. 126 (2004) 12847–12855. [DOI] [PMID: 15469281]
[EC 1.17.7.4 created 2003 as EC 1.17.1.2, modified 2009, transferred 2016 to EC 1.17.7.4]
 
 
EC 2.2.1.7     
Accepted name: 1-deoxy-D-xylulose-5-phosphate synthase
Reaction: pyruvate + D-glyceraldehyde 3-phosphate = 1-deoxy-D-xylulose 5-phosphate + CO2
For diagram of non-mevalonate terpenoid biosynthesis, click here and for mechanism of reaction, click here
Glossary: thiamine diphosphate = 3-[(4-amino-2-methylpyrimidin-5-yl)methyl]-5-(2-diphosphoethyl)-4-methyl-1,3-thiazolium
Other name(s): 1-deoxy-D-xylulose-5-phosphate pyruvate-lyase (carboxylating); DXP-synthase
Systematic name: pyruvate:D-glyceraldehyde-3-phosphate acetaldehydetransferase (decarboxylating)
Comments: Requires thiamine diphosphate. The enzyme forms part of an alternative nonmevalonate pathway for terpenoid biosynthesis (for diagram, click here).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 202218-79-9
References:
1.  Sprenger, G.A., Schörken, U., Weigert, T., Grolle, S., deGraaf, A.A., Taylor, S.V., Begley, T.P., Bringer-Meyer, S. and Sahm, H. Identification of a thiamin-dependent synthase in Escherichia coli required for the formation of the 1-deoxy-D-xylulose 5-phosphate precursor to isoprenoids, thiamin, and pyridoxol. Proc. Natl. Acad. Sci. USA 94 (1997) 12857–12862. [DOI] [PMID: 9371765]
2.  Kuzuyama, T., Takagi, M., Takahashi, S. and Seto, H. Cloning and characterization of 1-deoxy-D-xylulose 5-phosphate synthase from Streptomyces sp. strain CL190, which uses both the mevalonate and nonmevalonate pathways for isopentenyl diphosphate biosynthesis. J. Bacteriol. 182 (2000) 891–897. [DOI] [PMID: 10648511]
[EC 2.2.1.7 created 2001 as EC 4.1.3.37 transferred 2002 to EC 2.2.1.7]
 
 
EC 2.5.1.1     
Accepted name: dimethylallyltranstransferase
Reaction: dimethylallyl diphosphate + isopentenyl diphosphate = diphosphate + geranyl diphosphate
For diagram of terpenoid biosynthesis, click here
Other name(s): geranyl-diphosphate synthase; prenyltransferase; dimethylallyltransferase; DMAPP:IPP-dimethylallyltransferase; (2E,6E)-farnesyl diphosphate synthetase; diprenyltransferase; geranyl pyrophosphate synthase; geranyl pyrophosphate synthetase; trans-farnesyl pyrophosphate synthetase
Systematic name: dimethylallyl-diphosphate:isopentenyl-diphosphate dimethylallyltranstransferase
Comments: This enzyme will not accept larger prenyl diphosphates as efficient donors.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9032-79-5
References:
1.  Banthorpe, D.V., Bucknall, G.A., Doonan, H.J., Doonan, S. and Rowan, M.G. Biosynthesis of geraniol and nerol in cell-free extracts of Tanacetum vulgare. Phytochemistry 15 (1976) 91–100.
2.  Sagami, H., Ogura, K., Seto, S. and Kurokawa, T. A new prenyltransferase from Micrococcus lysodeikticus. Biochem. Biophys. Res. Commun. 85 (1978) 572–578. [DOI] [PMID: 736921]
[EC 2.5.1.1 created 1961]
 
 
EC 2.5.1.8      
Transferred entry: tRNA isopentenyltransferase. As it is now known that the substrate is dimethylallyl diphosphate, the enzyme has been transferred to EC 2.5.1.75, tRNA dimethylallyltransferase
[EC 2.5.1.8 created 1972, deleted 2009]
 
 
EC 2.5.1.10     
Accepted name: (2E,6E)-farnesyl diphosphate synthase
Reaction: geranyl diphosphate + isopentenyl diphosphate = diphosphate + (2E,6E)-farnesyl diphosphate
For diagram of terpenoid biosynthesis, click here
Other name(s): farnesyl-diphosphate synthase; geranyl transferase I; prenyltransferase; farnesyl pyrophosphate synthetase; farnesylpyrophosphate synthetase; geranyltranstransferase
Systematic name: geranyl-diphosphate:isopentenyl-diphosphate geranyltranstransferase
Comments: Some forms of this enzyme will also use dimethylallyl diphosphate as a substrate. The enzyme will not accept larger prenyl diphosphates as efficient donors.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37277-79-5
References:
1.  Lynen, F., Agranoff, B.W., Eggerer, H., Henning, V. and Möslein, E.M. Zur Biosynthese der Terpene. VI. γ,γ-Dimethyl-allyl-pyrophosphat und Geranyl-pyrophosphat, biologische Vorstufen des Squalens. Angew. Chem. 71 (1959) 657–663.
2.  Ogura, K., Nishino, T. and Seto, S. The purification of prenyltransferase and isopentenyl pyrophosphate isomerase of pumpkin fruit and their some properties. J. Biochem. (Tokyo) 64 (1968) 197–203. [PMID: 4303505]
3.  Reed, B.C. and Rilling, H. Crystallization and partial characterization of prenyltransferase from avian liver. Biochemistry 14 (1975) 50–54. [PMID: 1109590]
4.  Takahashi, I. and Ogura, K. Farnesyl pyrophosphate synthetase from Bacillus subtilis. J. Biochem. (Tokyo) 89 (1981) 1581–1587. [PMID: 6792191]
5.  Takahashi, I. and Ogura, K. Prenyltransferases of Bacillus subtilis: undecaprenyl pyrophosphate synthetase and geranylgeranyl pyrophosphate synthetase. J. Biochem. (Tokyo) 92 (1982) 1527–1537. [PMID: 6818223]
[EC 2.5.1.10 created 1972, modified 2010]
 
 
EC 2.5.1.11      
Transferred entry: trans-octaprenyltranstransferase. Now covered by EC 2.5.1.84 (all-trans-nonaprenyl-diphosphate synthase [geranyl-diphosphate specific]) and EC 2.5.1.85 (all-trans-nonaprenyl diphosphate synthase [geranylgeranyl-diphosphate specific])
[EC 2.5.1.11 created 1972, deleted 2010]
 
 
EC 2.5.1.20     
Accepted name: rubber cis-polyprenylcistransferase
Reaction: polycis-polyprenyl diphosphate + isopentenyl diphosphate = diphosphate + a polycis-polyprenyl diphosphate longer by one C5 unit
For diagram of all-cis-polyprenyl diphosphate, click here
Other name(s): rubber allyltransferase; rubber transferase; isopentenyl pyrophosphate cis-1,4-polyisoprenyl transferase; cis-prenyl transferase; rubber polymerase; rubber prenyltransferase
Systematic name: polycis-polyprenyl-diphosphate:isopentenyl-diphosphate polyprenylcistransferase
Comments: Rubber particles act as acceptor.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 62213-41-6
References:
1.  Archer, B.L. and Cockbain, E.G. Rubber transferase from Hevea brasiliensis latex. Methods Enzymol. 15 (1969) 476–480.
2.  McMullen, A.I. and McSweeney, G.P. The biosynthesis of rubber. Incorporation of isopentenyl pyrophosphate into purified rubber particles by a soluble latex-serum enzyme. Biochem. J. 101 (1966) 42–47. [PMID: 16742418]
[EC 2.5.1.20 created 1976]
 
 
EC 2.5.1.28     
Accepted name: dimethylallylcistransferase
Reaction: dimethylallyl diphosphate + isopentenyl diphosphate = diphosphate + neryl diphosphate
For diagram of all-cis-polyprenyl diphosphate, click here
Other name(s): neryl-diphosphate synthase
Systematic name: dimethylallyl-diphosphate:isopentenyl-diphosphate dimethylallylcistransferase
Comments: This enzyme will not use larger prenyl diphosphates as efficient donors.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9032-79-5
References:
1.  Banthorpe, D.V., Bucknall, G.A., Doonan, H.J., Doonan, S. and Rowan, M.G. Biosynthesis of geraniol and nerol in cell-free extracts of Tanacetum vulgare. Phytochemistry 15 (1976) 91–100.
2.  Beytía, E., Valenzuela, P. and Cori, O. Terpene biosynthesis: formation of nerol, geraniol, and other prenols by an enzyme system from Pinus radiata seedlings. Arch. Biochem. Biophys. 129 (1969) 346–356. [DOI] [PMID: 4303098]
[EC 2.5.1.28 created 1984]
 
 
EC 2.5.1.29     
Accepted name: geranylgeranyl diphosphate synthase
Reaction: (2E,6E)-farnesyl diphosphate + isopentenyl diphosphate = diphosphate + geranylgeranyl diphosphate
For diagram of terpenoid biosynthesis, click here
Other name(s): geranylgeranyl-diphosphate synthase; geranylgeranyl pyrophosphate synthetase; geranylgeranyl-PP synthetase; farnesyltransferase; geranylgeranyl pyrophosphate synthase; farnesyltranstransferase (obsolete)
Systematic name: (2E,6E)-farnesyl-diphosphate:isopentenyl-diphosphate farnesyltranstransferase
Comments: Some forms of this enzyme will also use geranyl diphosphate and dimethylallyl diphosphate as donors; it will not use larger prenyl diphosphates as efficient donors.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9032-58-0
References:
1.  Sagami, H., Ishi, K. and Ogura, K. Occurrence and unusual properties of geranylgeranyl pyrophosphate synthetase of pig liver. Biochem. Int. 3 (1981) 669–675.
[EC 2.5.1.29 created 1984, modified 2011]
 
 
EC 2.5.1.30     
Accepted name: heptaprenyl diphosphate synthase
Reaction: (2E,6E)-farnesyl diphosphate + 4 isopentenyl diphosphate = 4 diphosphate + all-trans-heptaprenyl diphosphate
For diagram of terpenoid biosynthesis, click here
Other name(s): all-trans-heptaprenyl-diphosphate synthase; heptaprenyl pyrophosphate synthase; heptaprenyl pyrophosphate synthetase; HepPP synthase; HepPS; heptaprenylpyrophosphate synthetase
Systematic name: (2E,6E)-farnesyl-diphosphate:isopentenyl-diphosphate farnesyltranstransferase (adding 4 isopentenyl units)
Comments: This enzyme catalyses the condensation reactions resulting in the formation of all-trans-heptaprenyl diphosphate, the isoprenoid side chain of ubiquinone-7 and menaquinone-7. The enzyme adds four isopentenyl diphosphate molecules sequentially to farnesyl diphosphate with trans stereochemistry.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 74506-59-5
References:
1.  Takahashi, I., Ogura, K. and Seto, S. Heptaprenyl pyrophosphate synthetase from Bacillus subtilis. J. Biol. Chem. 255 (1980) 4539–4543. [PMID: 6768722]
2.  Zhang, Y.W., Koyama, T., Marecak, D.M., Prestwich, G.D., Maki, Y. and Ogura, K. Two subunits of heptaprenyl diphosphate synthase of Bacillus subtilis form a catalytically active complex. Biochemistry 37 (1998) 13411–13420. [DOI] [PMID: 9748348]
3.  Zhang, Y.W., Li, X.Y., Sugawara, H. and Koyama, T. Site-directed mutagenesis of the conserved residues in component I of Bacillus subtilis heptaprenyl diphosphate synthase. Biochemistry 38 (1999) 14638–14643. [DOI] [PMID: 10545188]
4.  Suzuki, T., Zhang, Y.W., Koyama, T., Sasaki, D.Y. and Kurihara, K. Direct observation of substrate-enzyme complexation by surface forces measurement. J. Am. Chem. Soc. 128 (2006) 15209–15214. [DOI] [PMID: 17117872]
[EC 2.5.1.30 created 1984, modified 2010]
 
 
EC 2.5.1.31     
Accepted name: ditrans,polycis-undecaprenyl-diphosphate synthase [(2E,6E)-farnesyl-diphosphate specific]
Reaction: (2E,6E)-farnesyl diphosphate + 8 isopentenyl diphosphate = 8 diphosphate + ditrans,octacis-undecaprenyl diphosphate
For diagram of di- and tritrans,polycis-polyprenol biosynthesis, click here
Other name(s): di-trans,poly-cis-undecaprenyl-diphosphate synthase; undecaprenyl-diphosphate synthase; bactoprenyl-diphosphate synthase; UPP synthetase; undecaprenyl diphosphate synthetase; undecaprenyl pyrophosphate synthetase; di-trans,poly-cis-decaprenylcistransferase
Systematic name: (2E,6E)-farnesyl-diphosphate:isopentenyl-diphosphate cistransferase (adding 8 isopentenyl units)
Comments: Undecaprenyl pyrophosphate synthase catalyses the consecutive condensation reactions of a farnesyl diphosphate with eight isopentenyl diphosphates, in which new cis-double bonds are formed, to generate undecaprenyl diphosphate that serves as a lipid carrier for peptidoglycan synthesis of bacterial cell wall [3].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 52350-87-5
References:
1.  Muth, J.D. and Allen, C.M. Undecaprenyl pyrophosphate synthetase from Lactobacillus plantarum: a dimeric protein. Arch. Biochem. Biophys. 230 (1984) 49–60. [DOI] [PMID: 6712246]
2.  Takahashi, I. and Ogura, K. Prenyltransferases of Bacillus subtilis: undecaprenyl pyrophosphate synthetase and geranylgeranyl pyrophosphate synthetase. J. Biochem. (Tokyo) 92 (1982) 1527–1537. [PMID: 6818223]
3.  Guo, R.T., Ko, T.P., Chen, A.P., Kuo, C.J., Wang, A.H. and Liang, P.H. Crystal structures of undecaprenyl pyrophosphate synthase in complex with magnesium, isopentenyl pyrophosphate, and farnesyl thiopyrophosphate: roles of the metal ion and conserved residues in catalysis. J. Biol. Chem. 280 (2005) 20762–20774. [DOI] [PMID: 15788389]
4.  Ko, T.P., Chen, Y.K., Robinson, H., Tsai, P.C., Gao, Y.G., Chen, A.P., Wang, A.H. and Liang, P.H. Mechanism of product chain length determination and the role of a flexible loop in Escherichia coli undecaprenyl-pyrophosphate synthase catalysis. J. Biol. Chem. 276 (2001) 47474–47482. [DOI] [PMID: 11581264]
5.  Fujikura, K., Zhang, Y.W., Fujihashi, M., Miki, K. and Koyama, T. Mutational analysis of allylic substrate binding site of Micrococcus luteus B-P 26 undecaprenyl diphosphate synthase. Biochemistry 42 (2003) 4035–4041. [DOI] [PMID: 12680756]
6.  Fujihashi, M., Zhang, Y.W., Higuchi, Y., Li, X.Y., Koyama, T. and Miki, K. Crystal structure of cis-prenyl chain elongating enzyme, undecaprenyl diphosphate synthase. Proc. Natl. Acad. Sci. USA 98 (2001) 4337–4342. [DOI] [PMID: 11287651]
7.  Pan, J.J., Chiou, S.T. and Liang, P.H. Product distribution and pre-steady-state kinetic analysis of Escherichia coli undecaprenyl pyrophosphate synthase reaction. Biochemistry 39 (2000) 10936–10942. [DOI] [PMID: 10978182]
8.  Kharel, Y., Zhang, Y.W., Fujihashi, M., Miki, K. and Koyama, T. Significance of highly conserved aromatic residues in Micrococcus luteus B-P 26 undecaprenyl diphosphate synthase. J. Biochem. 134 (2003) 819–826. [PMID: 14769870]
[EC 2.5.1.31 created 1984, modified 2011]
 
 
EC 2.5.1.33      
Transferred entry: trans-pentaprenyltranstransferase. Now covered by EC 2.5.1.82 (hexaprenyl diphosphate synthase [geranylgeranyl-diphosphate specific]) and EC 2.5.1.83 (hexaprenyl-diphosphate synthase [(2E,6E)-farnesyl-diphosphate specific])
[EC 2.5.1.33 created 1984, deleted 2010]
 
 
EC 2.5.1.68     
Accepted name: (2Z,6E)-farnesyl diphosphate synthase
Reaction: geranyl diphosphate + isopentenyl diphosphate = diphosphate + (2Z,6E)-farnesyl diphosphate
For diagram of trans-polycis-polyprenol diphosphate biosynthesis, click here
Other name(s): (Z)-farnesyl diphosphate synthase; Z-farnesyl diphosphate synthase
Systematic name: geranyl-diphosphate:isopentenyl-diphosphate geranylcistransferase
Comments: Requires Mg2+ or Mn2+ for activity. The product of this reaction is an intermediate in the synthesis of decaprenyl phosphate, which plays a central role in the biosynthesis of most features of the mycobacterial cell wall, including peptidoglycan, linker unit galactan and arabinan. Neryl diphosphate can also act as substrate.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Schulbach, M.C., Mahapatra, S., Macchia, M., Barontini, S., Papi, C., Minutolo, F., Bertini, S., Brennan, P.J. and Crick, D.C. Purification, enzymatic characterization, and inhibition of the Z-farnesyl diphosphate synthase from Mycobacterium tuberculosis. J. Biol. Chem. 276 (2001) 11624–11630. [DOI] [PMID: 11152452]
[EC 2.5.1.68 created 2007, modified 2010]
 
 
EC 2.5.1.69     
Accepted name: lavandulyl diphosphate synthase
Reaction: 2 dimethylallyl diphosphate = diphosphate + lavandulyl diphosphate
For diagram of reaction, click here
Other name(s): FDS-5
Systematic name: dimethylallyl-diphosphate:dimethylallyl-diphosphate dimethylallyltransferase (lavandulyl-diphosphate-forming)
Comments: Lavandulyl diphosphate is a monoterpene with a non-head-to-tail linkage. It is unlike most monoterpenoids, which are derived from geranyl diphosphate and have isoprene units that are linked head-to-tail. When this enzyme is incubated with dimethylallyl diphosphate and isopentenyl diphosphate, it also forms the regular monoterpene geranyl diphosphate [2]. The enzyme from Artemisia tridentata (big sagebrush) forms both lavandulyl diphosphate and chrysanthemyl diphosphate (see EC 2.5.1.67, chrysanthemyl diphosphate synthase) when dimethylally diphosphate is the sole substrate.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Erickson, H.K. and Poulter, C.D. Chrysanthemyl diphosphate synthase. The relationship among chain elongation, branching, and cyclopropanation reactions in the isoprenoid biosynthetic pathway. J. Am. Chem. Soc. 125 (2003) 6886–6888. [DOI] [PMID: 12783539]
2.  Hemmerlin, A., Rivera, S.B., Erickson, H.K. and Poulter, C.D. Enzymes encoded by the farnesyl diphosphate synthase gene family in the Big Sagebrush Artemisia tridentata ssp. spiciformis. J. Biol. Chem. 278 (2003) 32132–32140. [DOI] [PMID: 12782626]
[EC 2.5.1.69 created 2007]
 
 
EC 2.5.1.71     
Accepted name: leachianone-G 2′′-dimethylallyltransferase
Reaction: dimethylallyl diphosphate + leachianone G = diphosphate + sophoraflavanone G
For diagram of sophoraflavanone-G biosynthesis, click here
Glossary: leachianone G = (-)-(2S)-2′-hydroxy-8-dimethylallylnaringenin = (-)-(2S)-5,7-dihydroxy-8-(2-hydroxy-3-methylbut-2-enyl)-2-(4-hydroxyphenyl)chroman-4-one
sophoraflavanone G = 2-{[(2S)-2-(2,4-dihydroxyphenyl)-5,7-dihydroxy-4-oxo-chroman-8-yl]methyl}-5-methyl-hex-4-enoic acid
Other name(s): LG 2′′-dimethylallyltransferase; leachianone G 2′′-dimethylallyltransferase; LGDT
Systematic name: dimethylallyl-diphosphate:leachianone-G 2′′-dimethylallyltransferase
Comments: This membrane-bound enzyme is located in the plastids and requires Mg2+ for activity. The reaction forms the lavandulyl sidechain of sophoraflavanone G by transferring a dimethylallyl group to the 2′′ position of another dimethylallyl group attached at postiion 8 of leachianone G. The enzyme is specific for dimethylallyl diphosphate as the prenyl donor, as it cannot be replaced by isopentenyl diphosphate or geranyl diphosphate. Euchrenone a7 (a 5-deoxy derivative of leachianone G) and kenusanone I (a 7-methoxy derivative of leachianone G) can also act as substrates, but more slowly. Along with EC 1.14.13.103 (8-dimethylallylnaringenin 2′-hydroxylase) and EC 2.5.1.70 (naringenin 8-dimethylallyltransferase), this enzyme forms part of the sophoraflavanone-G-biosynthesis pathway.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Zhao, P., Inoue, K., Kouno, I. and Yamamoto, H. Characterization of leachianone G 2′′-dimethylallyltransferase, a novel prenyl side-chain elongation enzyme for the formation of the lavandulyl group of sophoraflavanone G in Sophora flavescens Ait. cell suspension cultures. Plant Physiol. 133 (2003) 1306–1313. [DOI] [PMID: 14551337]
[EC 2.5.1.71 created 2007]
 
 
EC 2.5.1.75     
Accepted name: tRNA dimethylallyltransferase
Reaction: dimethylallyl diphosphate + adenine37 in tRNA = diphosphate + N6-dimethylallyladenine37 in tRNA
For diagram of N6-(Dimethylallyl)adenosine37 modified tTNA biosynthesis, click here
Other name(s): tRNA prenyltransferase; MiaA; transfer ribonucleate isopentenyltransferase (incorrect); Δ2-isopentenyl pyrophosphate:tRNA-Δ2-isopentenyl transferase (incorrect); Δ2-isopentenyl pyrophosphate:transfer ribonucleic acid Δ2-isopentenyltransferase (incorrect); dimethylallyl-diphosphate: tRNA dimethylallyltransferase
Systematic name: dimethylallyl-diphosphate:adenine37 in tRNA dimethylallyltransferase
Comments: Formerly known as tRNA isopentenyltransferase (EC 2.5.1.8), but it is now known that dimethylallyl diphosphate, rather than isopentenyl diphosphate, is the substrate.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Leung, H.C., Chen, Y. and Winkler, M.E. Regulation of substrate recognition by the MiaA tRNA prenyltransferase modification enzyme of Escherichia coli K-12. J. Biol. Chem. 272 (1997) 13073–13083. [DOI] [PMID: 9148919]
2.  Soderberg, T. and Poulter, C.D. Escherichia coli dimethylallyl diphosphate:tRNA dimethylallyltransferase: essential elements for recognition of tRNA substrates within the anticodon stem-loop. Biochemistry 39 (2000) 6546–6553. [DOI] [PMID: 10828971]
3.  Moore, J.A., Mathis, J.R. and Poulter, C.D. Escherichia coli dimethylallyl diphosphate:tRNA dimethylallyltransferase: pre-steady-state kinetic studies. Biochim. Biophys. Acta 1479 (2000) 166–174. [DOI] [PMID: 11004538]
[EC 2.5.1.75 created 1972 as EC 2.5.1.8, transferred 2009 to EC 2.5.1.75]
 
 
EC 2.5.1.81     
Accepted name: geranylfarnesyl diphosphate synthase
Reaction: geranylgeranyl diphosphate + isopentenyl diphosphate = (2E,6E,10E,14E)-geranylfarnesyl diphosphate + diphosphate
For diagram of terpenoid biosynthesis, click here
Other name(s): FGPP synthase; (all-E) geranylfarnesyl diphosphate synthase; GFPS; Fgs
Systematic name: geranylgeranyl-diphosphate:isopentenyl-diphosphate transtransferase (adding 1 isopentenyl unit)
Comments: The enzyme from Methanosarcina mazei is involved in biosynthesis of the polyprenyl side-chain of methanophenazine, an electron carrier utilized for methanogenesis. It prefers geranylgeranyl diphosphate and farnesyl diphosphate as allylic substrate [1]. The enzyme from Aeropyrum pernix prefers farnesyl diphosphate as allylic substrate. The enzyme is involved in the biosynthesis of C25-C25 membrane lipids [2].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Ogawa, T., Yoshimura, T. and Hemmi, H. Geranylfarnesyl diphosphate synthase from Methanosarcina mazei: Different role, different evolution. Biochem. Biophys. Res. Commun. 393 (2010) 16–20. [DOI] [PMID: 20097171]
2.  Tachibana, A., Yano, Y., Otani, S., Nomura, N., Sako, Y. and Taniguchi, M. Novel prenyltransferase gene encoding farnesylgeranyl diphosphate synthase from a hyperthermophilic archaeon, Aeropyrum pernix. Molecular evolution with alteration in product specificity. Eur. J. Biochem. 267 (2000) 321–328. [DOI] [PMID: 10632701]
3.  Tachibana, A. A novel prenyltransferase, farnesylgeranyl diphosphate synthase, from the haloalkaliphilic archaeon, Natronobacterium pharaonis. FEBS Lett. 341 (1994) 291–294. [DOI] [PMID: 8137956]
4.  Lee, P.C., Mijts, B.N., Petri, R., Watts, K.T. and Schmidt-Dannert, C. Alteration of product specificity of Aeropyrum pernix farnesylgeranyl diphosphate synthase (Fgs) by directed evolution. Protein Eng. Des. Sel. 17 (2004) 771–777. [DOI] [PMID: 15548566]
[EC 2.5.1.81 created 2010]
 
 
EC 2.5.1.82     
Accepted name: hexaprenyl diphosphate synthase [geranylgeranyl-diphosphate specific]
Reaction: geranylgeranyl diphosphate + 2 isopentenyl diphosphate = 2 diphosphate + all-trans-hexaprenyl diphosphate
For diagram of terpenoid biosynthesis, click here
Other name(s): HexPS(ambiguous); (all-E) hexaprenyl diphosphate synthase; (all-trans) hexaprenyl diphosphate synthase; hexaprenyl pyrophosphate synthase (ambiguous); HexPPs (ambiguous); hexaprenyl diphosphate synthase (ambiguous)
Systematic name: geranylgeranyl-diphosphate:isopentenyl-diphosphate transferase (adding 2 isopentenyl units)
Comments: The enzyme prefers geranylgeranyl diphosphate to farnesyl diphosphate as an allylic substrate and does not show activity for geranyl diphosphate and dimethylallyl diphosphate. Requires Mg2+ [1].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Hemmi, H., Ikejiri, S., Yamashita, S. and Nishino, T. Novel medium-chain prenyl diphosphate synthase from the thermoacidophilic archaeon Sulfolobus solfataricus. J. Bacteriol. 184 (2002) 615–620. [DOI] [PMID: 11790729]
2.  Hemmi, H., Noike, M., Nakayama, T. and Nishino, T. Change of product specificity of hexaprenyl diphosphate synthase from Sulfolobus solfataricus by introducing mimetic mutations. Biochem. Biophys. Res. Commun. 297 (2002) 1096–1101. [DOI] [PMID: 12372398]
3.  Sun, H.Y., Ko, T.P., Kuo, C.J., Guo, R.T., Chou, C.C., Liang, P.H. and Wang, A.H. Homodimeric hexaprenyl pyrophosphate synthase from the thermoacidophilic crenarchaeon Sulfolobus solfataricus displays asymmetric subunit structures. J. Bacteriol. 187 (2005) 8137–8148. [DOI] [PMID: 16291686]
[EC 2.5.1.82 created 1984 as EC 2.5.1.33, part transferred 2010 to EC 2.5.1.82]
 
 
EC 2.5.1.83     
Accepted name: hexaprenyl diphosphate synthase [(2E,6E)-farnesyl-diphosphate specific]
Reaction: (2E,6E)-farnesyl diphosphate + 3 isopentenyl diphosphate = 3 diphosphate + all-trans-hexaprenyl diphosphate
For diagram of terpenoid biosynthesis, click here
Other name(s): HexPS (ambiguous); hexaprenyl pyrophosphate synthetase (ambiguous); hexaprenyl diphosphate synthase (ambiguous)
Systematic name: (2E,6E)-farnesyl-diphosphate:isopentenyl-diphosphate farnesyltranstransferase (adding 3 isopentenyl units)
Comments: The enzyme prefers farnesyl diphosphate to geranylgeranyl diphosphate as an allylic substrate and does not show activity for geranyl diphosphate and dimethylallyl diphosphate [1].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Fujii, H., Koyama, T. and Ogura, K. Hexaprenyl pyrophosphate synthetase from Micrococcus luteus B-P 26. Separation of two essential components. J. Biol. Chem. 257 (1982) 14610–14612. [PMID: 7174655]
2.  Shimizu, N., Koyama, T. and Ogura, K. Molecular cloning, expression, and characterization of the genes encoding the two essential protein components of Micrococcus luteus B-P 26 hexaprenyl diphosphate synthase. J. Bacteriol. 180 (1998) 1578–1581. [PMID: 9515931]
3.  Nagaki, M., Kimura, K., Kimura, H., Maki, Y., Goto, E., Nishino, T. and Koyama, T. Artificial substrates of medium-chain elongating enzymes, hexaprenyl- and heptaprenyl diphosphate synthases. Bioorg. Med. Chem. Lett. 11 (2001) 2157–2159. [DOI] [PMID: 11514159]
[EC 2.5.1.83 created 1984 as EC 2.5.1.33, part transferred 2010 to EC 2.5.1.83]
 
 
EC 2.5.1.84     
Accepted name: all-trans-nonaprenyl diphosphate synthase [geranyl-diphosphate specific]
Reaction: geranyl diphosphate + 7 isopentenyl diphosphate = 7 diphosphate + all-trans-nonaprenyl diphosphate
For diagram of terpenoid biosynthesis, click here
Glossary: solanesyl diphosphate = all-trans-nonaprenyl diphosphate
Other name(s): nonaprenyl diphosphate synthase (ambiguous); solanesyl diphosphate synthase (ambiguous); SolPP synthase (ambiguous); SPP-synthase (ambiguous); SPP synthase (ambiguous); solanesyl-diphosphate synthase (ambiguous); OsSPS2
Systematic name: geranyl-diphosphate:isopentenyl-diphosphate transtransferase (adding 7 isopentenyl units)
Comments: (2E,6E)-Farnesyl diphosphate and geranylgeranyl diphosphate are less effective as substrates than geranyl diphosphate. The enzyme is involved in the synthesis of the side chain of menaquinone-9 [1]. In Oryza sativa the enzyme SPS2 is involved in providing solanesyl diphosphate for plastoquinone-9 formation [3].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Sagami, H., Ogura, K. and Seto, S. Solanesyl pyrophosphate synthetase from Micrococcus lysodeikticus. Biochemistry 16 (1977) 4616–4622. [PMID: 911777]
2.  Fujii, H., Sagami, H., Koyama, T., Ogura, K., Seto, S., Baba, T. and Allen, C.M. Variable product specificity of solanesyl pyrophosphate synthetase. Biochem. Biophys. Res. Commun. 96 (1980) 1648–1653. [DOI] [PMID: 7447947]
3.  Ohara, K., Sasaki, K. and Yazaki, K. Two solanesyl diphosphate synthases with different subcellular localizations and their respective physiological roles in Oryza sativa. J. Exp. Bot. 61 (2010) 2683–2692. [DOI] [PMID: 20421194]
4.  Ohnuma, S., Koyama, T. and Ogura, K. Purification of solanesyl-diphosphate synthase from Micrococcus luteus. A new class of prenyltransferase. J. Biol. Chem. 266 (1991) 23706–23713. [PMID: 1748647]
5.  Gotoh, T., Koyama, T. and Ogura, K. Farnesyl diphosphate synthase and solanesyl diphosphate synthase reactions of diphosphate-modified allylic analogs: the significance of the diphosphate linkage involved in the allylic substrates for prenyltransferase. J. Biochem. 112 (1992) 20–27. [PMID: 1429508]
6.  Teclebrhan, H., Olsson, J., Swiezewska, E. and Dallner, G. Biosynthesis of the side chain of ubiquinone:trans-prenyltransferase in rat liver microsomes. J. Biol. Chem. 268 (1993) 23081–23086. [PMID: 8226825]
[EC 2.5.1.84 created 1972 as EC 2.5.1.11, part transferred 2010 to EC 2.5.1.84]
 
 
EC 2.5.1.85     
Accepted name: all-trans-nonaprenyl diphosphate synthase [geranylgeranyl-diphosphate specific]
Reaction: geranylgeranyl diphosphate + 5 isopentenyl diphosphate = 5 diphosphate + all-trans-nonaprenyl diphosphate
For diagram of terpenoid biosynthesis, click here
Glossary: solanesyl diphosphate = all-trans-nonaprenyll diphosphate
Other name(s): nonaprenyl diphosphate synthase (ambiguous); solanesyl diphosphate synthase (ambiguous); At-SPS2; At-SPS1; SPS1; SPS2
Systematic name: geranylgeranyl-diphosphate:isopentenyl-diphosphate transtransferase (adding 5 isopentenyl units)
Comments: Geranylgeranyl diphosphate is preferred over farnesyl diphosphate as allylic substrate [1]. The plant Arabidopsis thaliana has two different enzymes that catalyse this reaction. SPS1 contributes to the biosynthesis of the ubiquinone side-chain while SPS2 supplies the precursor of the plastoquinone side-chains [2].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Hirooka, K., Bamba, T., Fukusaki, E. and Kobayashi, A. Cloning and kinetic characterization of Arabidopsis thaliana solanesyl diphosphate synthase. Biochem. J. 370 (2003) 679–686. [DOI] [PMID: 12437513]
2.  Hirooka, K., Izumi, Y., An, C.I., Nakazawa, Y., Fukusaki, E. and Kobayashi, A. Functional analysis of two solanesyl diphosphate synthases from Arabidopsis thaliana. Biosci. Biotechnol. Biochem. 69 (2005) 592–601. [DOI] [PMID: 15784989]
3.  Jun, L., Saiki, R., Tatsumi, K., Nakagawa, T. and Kawamukai, M. Identification and subcellular localization of two solanesyl diphosphate synthases from Arabidopsis thaliana. Plant Cell Physiol. 45 (2004) 1882–1888. [DOI] [PMID: 15653808]
[EC 2.5.1.85 created 1972 as EC 2.5.1.11, part transferred 2010 to EC 2.5.1.85]
 
 
EC 2.5.1.86     
Accepted name: trans,polycis-decaprenyl diphosphate synthase
Reaction: (2Z,6E)-farnesyl diphosphate + 7 isopentenyl diphosphate = 7 diphosphate + trans,octacis-decaprenyl diphosphate
For diagram of trans,polycis-polyprenol diphosphate biosynthesis, click here
Other name(s): Rv2361c; (2Z,6Z,10Z,14Z,18Z,22Z,26Z,30Z,34E)-decaprenyl diphosphate synthase
Systematic name: (2Z,6E)-farnesyl-diphosphate:isopentenyl-diphosphate farnesylcistransferase (adding 7 isopentenyl units)
Comments: The enzyme is involved in the biosynthesis of decaprenyl phosphate, which plays a central role in the biosynthesis of essential mycobacterial cell wall components, such as the mycolyl-arabinogalactan-peptidoglycan complex and lipoarabinomannan [2].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Kaur, D., Brennan, P.J. and Crick, D.C. Decaprenyl diphosphate synthesis in Mycobacterium tuberculosis. J. Bacteriol. 186 (2004) 7564–7570. [DOI] [PMID: 15516568]
2.  Wang, W., Dong, C., McNeil, M., Kaur, D., Mahapatra, S., Crick, D.C. and Naismith, J.H. The structural basis of chain length control in Rv1086. J. Mol. Biol. 381 (2008) 129–140. [DOI] [PMID: 18597781]
3.  Crick, D.C., Schulbach, M.C., Zink, E.E., Macchia, M., Barontini, S., Besra, G.S. and Brennan, P.J. Polyprenyl phosphate biosynthesis in Mycobacterium tuberculosis and Mycobacterium smegmatis. J. Bacteriol. 182 (2000) 5771–5778. [DOI] [PMID: 11004176]
[EC 2.5.1.86 created 2010]
 
 
EC 2.5.1.87     
Accepted name: ditrans,polycis-polyprenyl diphosphate synthase [(2E,6E)-farnesyl diphosphate specific]
Reaction: (2E,6E)-farnesyl diphosphate + n isopentenyl diphosphate = n diphosphate + ditrans,polycis-polyprenyl diphosphate (n = 10–55)
For diagram of di- and tritrans,polycis-polyprenol biosynthesis, click here
Other name(s): RER2; Rer2p; Rer2p Z-prenyltransferase; Srt1p; Srt2p Z-prenyltransferase; ACPT; dehydrodolichyl diphosphate synthase 1
Systematic name: (2E,6E)-farnesyl-diphosphate:isopentenyl-diphosphate cistransferase (adding 10–55 isopentenyl units)
Comments: The enzyme is involved in biosynthesis of dolichol (a long-chain polyprenol) with a saturated α-isoprene unit, which serves as a glycosyl carrier in protein glycosylation [1]. The yeast Saccharomyces cerevisiae has two different enzymes that catalyse this reaction. Rer2p synthesizes a well-defined family of polyprenols of 13–18 isoprene residues with dominating C80 (16 isoprene residues) extending to C120, while Srt1p synthesizes mainly polyprenol with 22 isoprene subunits. Largest Srt1p products reach C290 [2]. The enzyme from Arabidopsis thaliana catalyses the formation of polyprenyl diphosphates with predominant carbon number C120 [4].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Sato, M., Fujisaki, S., Sato, K., Nishimura, Y. and Nakano, A. Yeast Saccharomyces cerevisiae has two cis-prenyltransferases with different properties and localizations. Implication for their distinct physiological roles in dolichol synthesis. Genes Cells 6 (2001) 495–506. [DOI] [PMID: 11442630]
2.  Poznanski, J. and Szkopinska, A. Precise bacterial polyprenol length control fails in Saccharomyces cerevisiae. Biopolymers 86 (2007) 155–164. [DOI] [PMID: 17345630]
3.  Sato, M., Sato, K., Nishikawa, S., Hirata, A., Kato, J. and Nakano, A. The yeast RER2 gene, identified by endoplasmic reticulum protein localization mutations, encodes cis-prenyltransferase, a key enzyme in dolichol synthesis. Mol. Cell Biol. 19 (1999) 471–483. [DOI] [PMID: 9858571]
4.  Oh, S.K., Han, K.H., Ryu, S.B. and Kang, H. Molecular cloning, expression, and functional analysis of a cis-prenyltransferase from Arabidopsis thaliana. Implications in rubber biosynthesis. J. Biol. Chem. 275 (2000) 18482–18488. [DOI] [PMID: 10764783]
5.  Cunillera, N., Arro, M., Fores, O., Manzano, D. and Ferrer, A. Characterization of dehydrodolichyl diphosphate synthase of Arabidopsis thaliana, a key enzyme in dolichol biosynthesis. FEBS Lett. 477 (2000) 170–174. [DOI] [PMID: 10908715]
[EC 2.5.1.87 created 2010]
 
 
EC 2.5.1.88     
Accepted name: trans,polycis-polyprenyl diphosphate synthase [(2Z,6E)-farnesyl diphosphate specific]
Reaction: (2Z,6E)-farnesyl diphosphate + n isopentenyl diphosphate = n diphosphate + trans,polycis-polyprenyl diphosphate (n = 9–11)
For diagram of trans-polycis-polyprenol diphosphate biosynthesis, click here
Systematic name: (2Z,6E)-farnesyl-diphosphate:isopentenyl-diphosphate cistransferase (adding 9–11 isopentenyl units)
Comments: Highest activity with (2Z,6E)-farnesyl diphosphate as allylic substrate. Broad product specificity with the major product being dodecaprenyl diphosphate. Synthesizes even C70 prenyl diphosphate as the maximum chain-length product [1].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Ambo, T., Noike, M., Kurokawa, H. and Koyama, T. Cloning and functional analysis of cis-prenyltransferase from Thermobifida fusca. J. Biosci. Bioeng. 107 (2009) 620–622. [DOI] [PMID: 19447338]
[EC 2.5.1.88 created 2010]
 
 
EC 2.5.1.89     
Accepted name: tritrans,polycis-undecaprenyl diphosphate synthase [geranylgeranyl-diphosphate specific]
Reaction: geranylgeranyl diphosphate + 7 isopentenyl diphosphate = 7 diphosphate + tritrans,heptacis-undecaprenyl diphosphate
For diagram of di- and tritrans,polycis-polyprenol biosynthesis, click here
Systematic name: geranylgeranyl-diphosphate:isopentenyl-diphosphate cistransferase (adding 7 isopentenyl units)
Comments: This enzyme is involved in the biosynthesis of the glycosyl carrier lipid in some archaebacteria. Unlike EC 2.5.1.31, its counterpart in most bacteria, it prefers geranylgeranyl diphosphate to farnesyl diphosphate as the allylic substrate, resulting in production of a tritrans,polycis variant of undecaprenyl diphosphate [1].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Hemmi, H., Yamashita, S., Shimoyama, T., Nakayama, T. and Nishino, T. Cloning, expression, and characterization of cis-polyprenyl diphosphate synthase from the thermoacidophilic archaeon Sulfolobus acidocaldarius. J. Bacteriol. 183 (2001) 401–404. [DOI] [PMID: 11114943]
[EC 2.5.1.89 created 2010, modified 2011]
 
 
EC 2.5.1.90     
Accepted name: all-trans-octaprenyl-diphosphate synthase
Reaction: (2E,6E)-farnesyl diphosphate + 5 isopentenyl diphosphate = 5 diphosphate + all-trans-octaprenyl diphosphate
For diagram of terpenoid biosynthesis, click here
Glossary: all-trans-octaprenyl diphosphate = OPP
Other name(s): octaprenyl-diphosphate synthase; octaprenyl pyrophosphate synthetase; polyprenylpyrophosphate synthetase; terpenoidallyltransferase; terpenyl pyrophosphate synthetase; trans-heptaprenyltranstransferase; trans-prenyltransferase
Systematic name: (2E,6E)-farnesyl-diphosphate:isopentenyl-diphosphate farnesyltranstransferase (adding 5 isopentenyl units)
Comments: This enzyme catalyses the condensation reactions resulting in the formation of all-trans-octaprenyl diphosphate, the isoprenoid side chain of ubiquinone-8 and menaquinone-8. The enzyme adds five isopentenyl diphosphate molecules sequentially to farnesyl diphosphate with trans stereochemistry
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Fujisaki, S., Nishino, T. and Katsuki, H. Isoprenoid synthesis in Escherichia coli. Separation and partial purification of four enzymes involved in the synthesis. J. Biochem. 99 (1986) 1327–1337. [PMID: 3519603]
2.  Asai, K., Fujisaki, S., Nishimura, Y., Nishino, T., Okada, K., Nakagawa, T., Kawamukai, M. and Matsuda, H. The identification of Escherichia coli ispB (cel) gene encoding the octaprenyl diphosphate synthase. Biochem. Biophys. Res. Commun. 202 (1994) 340–345. [DOI] [PMID: 8037730]
[EC 2.5.1.90 created 2010]
 
 
EC 2.5.1.91     
Accepted name: all-trans-decaprenyl-diphosphate synthase
Reaction: (2E,6E)-farnesyl diphosphate + 7 isopentenyl diphosphate = 7 diphosphate + all-trans-decaprenyl diphosphate
For diagram of terpenoid biosynthesis, click here
Other name(s): decaprenyl-diphosphate synthase; decaprenyl pyrophosphate synthetase; polyprenylpyrophosphate synthetase; terpenoidallyltransferase; terpenyl pyrophosphate synthetase; trans-prenyltransferase
Systematic name: (2E,6E)-farnesyl-diphosphate:isopentenyl-diphosphate farnesyltranstransferase (adding 7 isopentenyl units)
Comments: This enzyme catalyses the condensation reactions resulting in the formation of all-trans-decaprenyl diphosphate, the isoprenoid side chain of ubiquinone-10 and menaquinone-10. The enzyme adds seven isopentenyl diphosphate molecules sequentially to farnesyl diphosphate with trans stereochemistry.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Saiki, R., Nagata, A., Kainou, T., Matsuda, H. and Kawamukai, M. Characterization of solanesyl and decaprenyl diphosphate synthases in mice and humans. FEBS J. 272 (2005) 5606–5622. [DOI] [PMID: 16262699]
[EC 2.5.1.91 created 2010]
 
 
EC 2.5.1.92     
Accepted name: (2Z,6Z)-farnesyl diphosphate synthase
Reaction: dimethylallyl diphosphate + 2 isopentenyl diphosphate = 2 diphosphate + (2Z,6Z)-farnesyl diphosphate
For diagram of all-cis-polyprenyl diphosphate, click here
Other name(s): cis,cis-farnesyl diphosphate synthase; Z,Z-FPP synthase; zFPS; Z,Z-farnesyl pyrophosphate synthase
Systematic name: dimethylallyl-diphosphate:isopentenyl-diphosphate cistransferase (adding 2 isopentenyl units)
Comments: This enzyme, originally characterized from wild tomato, specifically forms (2Z,6Z)-farnesyl diphosphate via neryl diphosphate and isopentenyl diphosphate. In wild tomato it is involved in the biosynthesis of several sesquiterpenes. See also EC 2.5.1.68 [(2Z,6E)-farnesyl diphosphate synthase] and EC 2.5.1.10 [(2E,6E)-farnesyl diphosphate synthase].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Sallaud, C., Rontein, D., Onillon, S., Jabes, F., Duffe, P., Giacalone, C., Thoraval, S., Escoffier, C., Herbette, G., Leonhardt, N., Causse, M. and Tissier, A. A novel pathway for sesquiterpene biosynthesis from Z,Z-farnesyl pyrophosphate in the wild tomato Solanum habrochaites. Plant Cell 21 (2009) 301–317. [DOI] [PMID: 19155349]
[EC 2.5.1.92 created 2010, modified 2011]
 
 
EC 2.5.1.142     
Accepted name: nerylneryl diphosphate synthase
Reaction: dimethylallyl diphosphate + 3 isopentenyl diphosphate = 3 diphosphate + nerylneryl diphosphate
For diagram of all-cis-polyprenyl diphosphate, click here
Glossary: nerylneryl diphosphate = all-cis-tetraprenyl diphosphate
Other name(s): CPT2
Systematic name: dimethylallyl-diphosphate:isopentenyl-diphosphate cistransferase (adding 3 isopentenyl units)
Comments: Isolated from the plant Solanum lycopersicum (tomato).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Akhtar, T.A., Matsuba, Y., Schauvinhold, I., Yu, G., Lees, H.A., Klein, S.E. and Pichersky, E. The tomato cis-prenyltransferase gene family. Plant J. 73 (2013) 640–652. [DOI] [PMID: 23134568]
2.  Matsuba, Y., Zi, J., Jones, A.D., Peters, R.J. and Pichersky, E. Biosynthesis of the diterpenoid lycosantalonol via nerylneryl diphosphate in Solanum lycopersicum. PLoS One 10:e0119302 (2015). [DOI] [PMID: 25786135]
[EC 2.5.1.142 created 2017]
 
 
EC 2.7.4.26     
Accepted name: isopentenyl phosphate kinase
Reaction: ATP + isopentenyl phosphate = ADP + isopentenyl diphosphate
For diagram of the archaeal mevalonate pathway, click here
Systematic name: ATP:isopentenyl phosphate phosphotransferase
Comments: The enzyme is involved in the mevalonate pathway in Archaea [1]. The activity has also been identified in the plant Mentha piperita (peppermint) [2]. It is strictly specific for ATP but can use other phosphate acceptors such as dimethylallyl phosphate, geranyl phosphate, or fosfomycin.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Grochowski, L.L., Xu, H. and White, R.H. Methanocaldococcus jannaschii uses a modified mevalonate pathway for biosynthesis of isopentenyl diphosphate. J. Bacteriol. 188 (2006) 3192–3198. [DOI] [PMID: 16621811]
2.  Lange, B.M. and Croteau, R. Isopentenyl diphosphate biosynthesis via a mevalonate-independent pathway: isopentenyl monophosphate kinase catalyzes the terminal enzymatic step. Proc. Natl. Acad. Sci. USA 96 (1999) 13714–13719. [DOI] [PMID: 10570138]
3.  Chen, M. and Poulter, C.D. Characterization of thermophilic archaeal isopentenyl phosphate kinases. Biochemistry 49 (2010) 207–217. [DOI] [PMID: 19928876]
4.  Mabanglo, M.F., Schubert, H.L., Chen, M., Hill, C.P. and Poulter, C.D. X-ray structures of isopentenyl phosphate kinase. ACS Chem. Biol. 5 (2010) 517–527. [DOI] [PMID: 20402538]
[EC 2.7.4.26 created 2012]
 
 
EC 4.1.1.33     
Accepted name: diphosphomevalonate decarboxylase
Reaction: ATP + (R)-5-diphosphomevalonate = ADP + phosphate + isopentenyl diphosphate + CO2
For diagram of terpenoid biosynthesis, click here
Other name(s): pyrophosphomevalonate decarboxylase; mevalonate-5-pyrophosphate decarboxylase; pyrophosphomevalonic acid decarboxylase; 5-pyrophosphomevalonate decarboxylase; mevalonate 5-diphosphate decarboxylase; ATP:(R)-5-diphosphomevalonate carboxy-lyase (dehydrating)
Systematic name: ATP:(R)-5-diphosphomevalonate carboxy-lyase (adding ATP; isopentenyl-diphosphate-forming)
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9024-66-2
References:
1.  Bloch, K., Chaykin, S., Phillips, A.H. and de Waard, A. Mevalonic acid pyrophosphate and isopentenyl pyrophosphate. J. Biol. Chem. 234 (1959) 2595–2604. [PMID: 13801508]
[EC 4.1.1.33 created 1961]
 
 
EC 4.2.3.26     
Accepted name: R-linalool synthase
Reaction: geranyl diphosphate + H2O = (3R)-linalool + diphosphate
For diagram of acyclic monoterpenoid biosynthesis, click here
Glossary: (3R)-linalool = (3R)-3,7-dimethylocta-1,6-dien-3-ol
Other name(s): (3R)-linalool synthase; (-)-3R-linalool synthase
Systematic name: geranyl-diphosphate diphosphate-lyase [(3R)-linalool-forming]
Comments: Geranyl diphosphate cannot be replaced by isopentenyl diphosphate, dimethylallyl diphosphate, farnesyl diphosphate or geranylgeranyl diphosphate as substrate [1]. Requires Mg2+ or Mn2+ for activity. Unlike many other monoterpene synthases, only a single product, (3R)-linalool, is formed.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 254993-26-5
References:
1.  Jia, J.W., Crock, J., Lu, S., Croteau, R. and Chen, X.Y. (3R)-Linalool synthase from Artemisia annua L.: cDNA isolation, characterization, and wound induction. Arch. Biochem. Biophys. 372 (1999) 143–149. [DOI] [PMID: 10562427]
2.  Crowell, A.L., Williams, D.C., Davis, E.M., Wildung, M.R. and Croteau, R. Molecular cloning and characterization of a new linalool synthase. Arch. Biochem. Biophys. 405 (2002) 112–121. [DOI] [PMID: 12176064]
[EC 4.2.3.26 created 2006]
 
 
EC 5.3.3.2     
Accepted name: isopentenyl-diphosphate Δ-isomerase
Reaction: isopentenyl diphosphate = dimethylallyl diphosphate
For diagram of terpenoid biosynthesis, click here
Other name(s): isopentenylpyrophosphate Δ-isomerase; methylbutenylpyrophosphate isomerase; isopentenylpyrophosphate isomerase
Systematic name: isopentenyl-diphosphate Δ32-isomerase
Comments: The enzyme from Streptomyces sp. strain CL190 requires FMN and NAD(P)H as cofactors. Activity is reduced if FMN is replaced by FAD, but the enzyme becomes inactive when NAD(P)H is replaced by NAD+ or NADP+. That enzyme also requires Mg2+, Mn2+ or Ca2+ for activity.
Links to other databases: BRENDA, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9033-27-6
References:
1.  Kaneda, K., Kuzuyama, T., Takagi, M., Hayakawa, Y. and Seto, H. An unusual isopentenyl diphosphate isomerase found in the mevalonate pathway gene cluster from Streptomyces sp. strain CL190. Proc. Natl. Acad. Sci. USA 98 (2001) 932–937. [DOI] [PMID: 11158573]
2.  Bishop, J.M. Cellular oncogenes and retroviruses. Annu. Rev. Biochem. 52 (1983) 301–354. [DOI] [PMID: 6351725]
3.  Agranoff, B.W., Eggerer, H., Henning, U. and Lynen, F. Biosynthesis of terpenes. VII. Isopentenyl pyrophosphate isomerase. J. Biol. Chem. 235 (1960) 326–332. [PMID: 13792054]
[EC 5.3.3.2 created 1961, modified 2002]
 
 


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