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Literature summary extracted from

  • Holmberg, N.; Harker, M.; Wallace, A.D.; Clayton, J.C.; Gibbard, C.L.; Safford, R.
    Co-expression of N-terminal truncated 3-hydroxy-3-methylglutaryl CoA reductase and C24-sterol methyltransferase type 1 in transgenic tobacco enhances carbon flux towards end-product sterols (2003), Plant J., 36, 12-20.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.1.1.34 construction of a N-terminally truncated enzyme, comprising the catalytic site, and subcloning into Escherichia coli strain DH5alpha Hevea brasiliensis
2.1.1.142 coexpression of the catalytic domain of Hevea brasiliensis 3-hydroxy-3-methylglutaryl CoA reductase and Nicotiana tabacum C24-sterol methyltransferase type 1 in tobacco, under control of both constitutive and seed-specific promoters, resulting in increased accumulation of total sterol in seed tissue by 2.5fold and 2.1fold, respectively Nicotiana tabacum

Protein Variants

EC Number Protein Variants Comment Organism
1.1.1.34 additional information coexpression of N-terminal truncated Hevea brasiliensis (S)-3-hydroxy-3-methylglutaryl CoA reductase and tobacco C24-sterol methyltransferase type 1 in transgenic Nicotiana tabacum plants enhances carbon flux towards end-product sterols, expression under control of both seed-specific and constitutive promotors leads to enhancement of sterol accumulation by 2.5 and 2.1fold, respectively, analysis of the sterol spectrum, overview Hevea brasiliensis

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.1.1.34 endoplasmic reticulum located on the cytoplasmic site, integrated into the membrane Hevea brasiliensis 5783
-
1.1.1.34 membrane integral Hevea brasiliensis 16020
-

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.1.1.34 (S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+ Hevea brasiliensis
-
 (R)-mevalonate + CoA + 2 NADP+
-
 ?
1.1.1.34 additional information Hevea brasiliensis enzyme plays a central role in sterol biosynthesis, investigation of the physiological regulation, 3-hydroxy-3-methylglutaryl CoA reductase and C24-sterol methyltransferase type 1 work in concert to control carbon flux into end-product sterols ?
-
 ?
2.1.1.142 S-adenosyl-L-methionine + 5alpha-cholesta-8,24-dien-3beta-ol Nicotiana tabacum 3-hydroxy-3-methylglutaryl CoA reductase and C24-sterol methyltransferase type 1 work in concert to control carbon flux into end-product sterols. Sterol composition can be controlled by the temporal activity of the promoters driving transgene expression S-adenosyl-L-homocysteine + 24-methylene-5alpha-cholest-8-en-3beta-ol
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.1.1.34 Hevea brasiliensis
-
-
-
2.1.1.142 Nicotiana tabacum
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.1.34 (S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
 Hevea brasiliensis (R)-mevalonate + CoA + 2 NADP+
-
 ?
1.1.1.34 additional information enzyme plays a central role in sterol biosynthesis, investigation of the physiological regulation, 3-hydroxy-3-methylglutaryl CoA reductase and C24-sterol methyltransferase type 1 work in concert to control carbon flux into end-product sterols Hevea brasiliensis ?
-
 ?
2.1.1.142 S-adenosyl-L-methionine + 5alpha-cholesta-8,24-dien-3beta-ol 3-hydroxy-3-methylglutaryl CoA reductase and C24-sterol methyltransferase type 1 work in concert to control carbon flux into end-product sterols. Sterol composition can be controlled by the temporal activity of the promoters driving transgene expression Nicotiana tabacum S-adenosyl-L-homocysteine + 24-methylene-5alpha-cholest-8-en-3beta-ol
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.1.1.34 3-hydroxy-3-methylglutaryl CoA reductase
-
 Hevea brasiliensis
1.1.1.34 HMGR
-
 Hevea brasiliensis
2.1.1.142 C24-sterol methyltransferase type 1
-
 Nicotiana tabacum
2.1.1.142 SMT1
-
 Nicotiana tabacum