2.5.1.93: 4-hydroxybenzoate geranyltransferase
This is an abbreviated version!
For detailed information about 4-hydroxybenzoate geranyltransferase, go to the full flat file.
Word Map on EC 2.5.1.93
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2.5.1.93
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shikonins
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naphthoquinone
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lithospermum
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euchroma
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arnebia
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erythrorhizon
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geranylation
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prenyltransferase
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hairy
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royle
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ubiquinone
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boraginaceae
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acetylshikonin
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mevalonate
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phenylpropanoid
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flask
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ammonia
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prenyl
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contigs
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pyrophosphate
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isobutyrylshikonin
- 2.5.1.93
- shikonins
- naphthoquinone
-
lithospermum
- euchroma
- arnebia
- erythrorhizon
-
geranylation
- prenyltransferase
-
hairy
-
royle
- ubiquinone
- boraginaceae
- acetylshikonin
- mevalonate
-
phenylpropanoid
-
flask
- ammonia
-
prenyl
-
contigs
- pyrophosphate
- isobutyrylshikonin
Reaction
Synonyms
4HB geranyltransferase, 4HB:geranyltransferase, AePGT, AePGT4, AePGT6, diphosphate:4-hydroxybenzoate geranyltransferase, geranyl diphosphate:4-hydroxybenzoate 3-geranyltransferase, geranyl diphosphate:4-hydroxybenzoate geranyltransferase, lepgt, LePGT-1, LePGT-2, LePGT1, p-hydroxybenzoate geranyltransferase, p-hydroxybenzoate-m-geranyltransferase, p-hydroxybenzoate: geranyltransferase, p-hydroxybenzoate:geranyltransferase, PGT, PGT-1, PHB geranyltransferase, PHBA geranyltransferase
ECTree
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Engineering
Engineering on EC 2.5.1.93 - 4-hydroxybenzoate geranyltransferase
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D212A
D87A
additional information
D212A
site-directed mutagenesis, the mutant shows almost no expression of the recombinant protein
D87A
site-directed mutagenesis, the mutant can be be successfully expressed, but is catalytically inactive
the amino acid residues of LePGT1 critical for the enzymatic activity and the region responsible for the binding of the substrates are elucidated by mutational analysis. Substrate specificity is analysed using chimeric enzymes derived from LePGT1 and UbiA (EC 2.5.1.39). In vitro and in vivo analysis of the chimeras suggests that the determinant region for this specificity is within 130 amino acids of the N-terminal
additional information
the substitution of aspartate with alanine, especially D87 and D212, causes a dramatic decrease in enzyme activity