phenylalanine and 3,3-dimethylallyl pyrophosphate

phenylalanine has been researched along with 3,3-dimethylallyl pyrophosphate in 2 studies

Research

Studies (2)

Timeframe	Studies, this research(%)	All Research%
pre-1990	0 (0.00)	18.7374
1990's	1 (50.00)	18.2507
2000's	0 (0.00)	29.6817
2010's	1 (50.00)	24.3611
2020's	0 (0.00)	2.80

Authors

Authors	Studies
Koyama, T; Nishino, T; Ogura, K; Tajima, M	1
Poulter, CD; Rudolf, JD	1

Other Studies

2 other study(ies) available for phenylalanine and 3,3-dimethylallyl pyrophosphate

Article	Year
Significance of Phe-220 and Gln-221 in the catalytic mechanism of farnesyl diphosphate synthase of Bacillus stearothermophilus. Biochemical and biophysical research communications, 1995, Jul-17, Volume: 212, Issue:2 Topics: Alkyl and Aryl Transferases; Amino Acid Sequence; Base Sequence; Binding Sites; Catalysis; Geobacillus stearothermophilus; Geranyltranstransferase; Glutamine; Hemiterpenes; Molecular Sequence Data; Mutagenesis, Site-Directed; Organophosphorus Compounds; Phenylalanine; Polyisoprenyl Phosphates; Structure-Activity Relationship; Transferases	1995
Tyrosine O-prenyltransferase SirD catalyzes S-, C-, and N-prenylations on tyrosine and tryptophan derivatives. ACS chemical biology, 2013, Dec-20, Volume: 8, Issue:12 Topics: Dimethylallyltranstransferase; Escherichia coli; Fungal Proteins; Gene Expression; Hemiterpenes; Kinetics; Organophosphorus Compounds; Phenylalanine; Piperazines; Prenylation; Recombinant Proteins; Saccharomycetales; Substrate Specificity; Sulfhydryl Compounds; Tryptophan; Tyrosine	2013

Article

Year

Significance of Phe-220 and Gln-221 in the catalytic mechanism of farnesyl diphosphate synthase of Bacillus stearothermophilus.

Biochemical and biophysical research communications, 1995, Jul-17, Volume: 212, Issue:2

Topics: Alkyl and Aryl Transferases; Amino Acid Sequence; Base Sequence; Binding Sites; Catalysis; Geobacillus stearothermophilus; Geranyltranstransferase; Glutamine; Hemiterpenes; Molecular Sequence Data; Mutagenesis, Site-Directed; Organophosphorus Compounds; Phenylalanine; Polyisoprenyl Phosphates; Structure-Activity Relationship; Transferases

1995

Tyrosine O-prenyltransferase SirD catalyzes S-, C-, and N-prenylations on tyrosine and tryptophan derivatives.

ACS chemical biology, 2013, Dec-20, Volume: 8, Issue:12

Topics: Dimethylallyltranstransferase; Escherichia coli; Fungal Proteins; Gene Expression; Hemiterpenes; Kinetics; Organophosphorus Compounds; Phenylalanine; Piperazines; Prenylation; Recombinant Proteins; Saccharomycetales; Substrate Specificity; Sulfhydryl Compounds; Tryptophan; Tyrosine

2013