3.7.1.7: beta-diketone hydrolase
This is an abbreviated version!
For detailed information about beta-diketone hydrolase, go to the full flat file.
Word Map on EC 3.7.1.7
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3.7.1.7
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sphingopyxis
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textile
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putida
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lipase
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sludge
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shake
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cytochemically
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ache
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desizing
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acetylacetone
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gly-x-ser-x-gly
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p-nitrophenyl
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alpha-granules
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caprylate
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industry
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wastewater
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hydrolysed
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pmsf
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sphingomonas
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depolymerases
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dt
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molecular biology
- 3.7.1.7
- sphingopyxis
-
textile
- putida
- lipase
-
sludge
-
shake
-
cytochemically
-
ache
-
desizing
- acetylacetone
-
gly-x-ser-x-gly
- p-nitrophenyl
-
alpha-granules
- caprylate
- industry
-
wastewater
-
hydrolysed
- pmsf
- sphingomonas
-
depolymerases
- dt
- molecular biology
Reaction
Synonyms
ABDH, Alr4455 protein, beta-diketone hydrolase, OPH, OPH hydrolase, oxidized polyvinyl alcohol hydrolase, oxidized PVA hydrolase, oxidized-PVA hydrolase, poly(vinyl alcohol) (PVA)-degrading enzyme, pOPH, PVA-degrading enzyme, PVAase, sOPH
ECTree
Advanced search results
Engineering
Engineering on EC 3.7.1.7 - beta-diketone hydrolase
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S172A
S172C
S172A
S172C
C241A/C248A
site-directed mutagenesis, the mutant shows unaltered activity compared to the wild-type enzyme
additional information
site-directed mutagenesis, the mutant shows 20% activity compared to the wild-type enzyme
S172A
site-directed mutagenesis, the mutant shows 20% activity compared to the wild-type enzyme, structure comarison with the wild-type enzyme
S172C
site-directed mutagenesis, the mutant shows less than 10% activity compared to the wild-type enzyme, structure comarison with the wild-type enzyme
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site-directed mutagenesis, the mutant shows 20% activity compared to the wild-type enzyme
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S172A
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site-directed mutagenesis, the mutant shows 20% activity compared to the wild-type enzyme, structure comarison with the wild-type enzyme
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S172C
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site-directed mutagenesis, the mutant shows less than 10% activity compared to the wild-type enzyme, structure comarison with the wild-type enzyme
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the mutants show reduced kcat/Km for 4-nitrophenyl acetate, indicating the importance of Trp255 in sequestering the active site from solvent. The significantly lower activity for 4-nitrophenyl butyrate can be a result of product inhibition. The mutant activity is retained with 4-nitrophenyl caprylate and 4-nitrophenyl laurate as the substrates, reflecting the amphipathic nature of the cleft
additional information
-
the mutants show reduced kcat/Km for 4-nitrophenyl acetate, indicating the importance of Trp255 in sequestering the active site from solvent. The significantly lower activity for 4-nitrophenyl butyrate can be a result of product inhibition. The mutant activity is retained with 4-nitrophenyl caprylate and 4-nitrophenyl laurate as the substrates, reflecting the amphipathic nature of the cleft
additional information
-
the mutants show reduced kcat/Km for 4-nitrophenyl acetate, indicating the importance of Trp255 in sequestering the active site from solvent. The significantly lower activity for 4-nitrophenyl butyrate can be a result of product inhibition. The mutant activity is retained with 4-nitrophenyl caprylate and 4-nitrophenyl laurate as the substrates, reflecting the amphipathic nature of the cleft
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