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Literature summary for 2.5.1.29 extracted from

  • Noike, M.; Katagiri, T.; Nakayama, T.; Nishino, T.; Hemmi, H.
    Effect of mutagenesis at the region upstream from the G(Q/E) motif of three types of geranylgeranyl diphosphate synthase on product chain-length (2009), J. Biosci. Bioeng., 107, 235-239.
    View publication on PubMed
Search for more literature for 2.5.1.29

Cloned(Commentary)

Cloned (Comment) Organism
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 Saccharomyces cerevisiae
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 Sulfolobus acidocaldarius
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 Pantoea ananatis

Protein Variants

Protein Variants Comment Organism
H139A mutation upstream from the G(Q/E) motif. Mutant forms larger condensation products than wild-type. With farnesyl diphosphate as allylic substrate, mutant produces large amounts of a C30 product Saccharomyces cerevisiae
I147A no change in chain length of product Sulfolobus acidocaldarius
I147A/S148A no change in chain length of product Sulfolobus acidocaldarius
I147F mutant does not accept farnesyl diphosphate as the allylic substrate, indicating a change in product specificity into that of farnesyl diphosphate synthase Sulfolobus acidocaldarius
I147G elongation in the chain length of product Sulfolobus acidocaldarius
L138A mutation upstream from the G(Q/E) motif. Mutant forms larger condensation products than wild-type. With farnesyl diphosphate as allylic substrate, mutant produces large amounts of a C25 product Saccharomyces cerevisiae
L162A nop change in chain length of product Pantoea ananatis
L162A/V163A altered substrate specificity, hardly accepts dimethylallyl diphosphate as substrate. Yields the products with the same chain-length with those of wild type Pantoea ananatis
R140A no enzymic activity Saccharomyces cerevisiae
S148A no change in chain length of product Sulfolobus acidocaldarius
S148F mutant does not accept farnesyl diphosphate as the allylic substrate, indicating a change in product specificity into that of farnesyl diphosphate synthase Sulfolobus acidocaldarius
S148G slight elongation in the chain length of product Sulfolobus acidocaldarius
S148H mutant does not accept farnesyl diphosphate as the allylic substrate, indicating a change in product specificity into that of farnesyl diphosphate synthase Sulfolobus acidocaldarius

Organism

Organism UniProt Comment Textmining
Pantoea ananatis
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 type II enzyme
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Saccharomyces cerevisiae
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 type III enzyme
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Sulfolobus acidocaldarius
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 type I enzyme
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(E,E)-farnesyl diphosphate + isopentenyl diphosphate
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 Sulfolobus acidocaldarius diphosphate + geranylgeranyl diphosphate
-
 ?
(E,E)-farnesyl diphosphate + isopentenyl diphosphate
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 Pantoea ananatis diphosphate + geranylgeranyl diphosphate
-
 ?
(E,E)-farnesyl diphosphate + isopentenyl diphosphate
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 Saccharomyces cerevisiae diphosphate + geranylgeranyl diphosphate mutants L138A and H139A synthesize larger products ?