Kamata S

References (2)

Title : Redesign of enzyme for improving catalytic activity and enantioselectivity toward poor substrates: manipulation of the transition state - Ema_2012_Org.Biomol.Chem_10_6299
Author(s) : Ema T , Nakano Y , Yoshida D , Kamata S , Sakai T
Ref : Org Biomol Chem , 10 :6299 , 2012
Abstract : Secondary alcohols having bulky substituents on both sides of the hydroxy group are inherently poor substrates for most lipases. In view of this weakness, we redesigned a Burkholderia cepacia lipase to create a variant with improved enzymatic characteristics. The I287F/I290A double mutant showed a high conversion and a high E value (>200) for a poor substrate for which the wild-type enzyme showed a low conversion and a low E value (5). This enhancement of catalytic activity and enantioselectivity of the variant resulted from the cooperative action of two mutations: Phe287 contributed to both enhancement of the (R)-enantiomer reactivity and suppression of the (S)-enantiomer reactivity, while Ala290 created a space to facilitate the acylation of the (R)-enantiomer. The kinetic constants indicated that the mutations effectively altered the transition state. Substrate mapping analysis strongly suggested that the CH/pi interaction partly enhanced the (R)-enantiomer reactivity, the estimated energy of the CH/pi interaction being -0.4 kcal mol(-1). The substrate scope of the I287F/I290A double mutant was broad. This biocatalyst was useful for the dynamic kinetic resolution of a variety of bulky secondary alcohols for which the wild-type enzyme shows little or no activity.
ESTHER : Ema_2012_Org.Biomol.Chem_10_6299
PubMedSearch : Ema_2012_Org.Biomol.Chem_10_6299
PubMedID: 22710791
Gene_locus related to this paper: burce-lipaa , burce-q75nt4

Title : Genome sequence of Kitasatospora setae NBRC 14216T: an evolutionary snapshot of the family Streptomycetaceae - Ichikawa_2010_DNA.Res_17_393
Author(s) : Ichikawa N , Oguchi A , Ikeda H , Ishikawa J , Kitani S , Watanabe Y , Nakamura S , Katano Y , Kishi E , Sasagawa M , Ankai A , Fukui S , Hashimoto Y , Kamata S , Otoguro M , Tanikawa S , Nihira T , Horinouchi S , Ohnishi Y , Hayakawa M , Kuzuyama T , Arisawa A , Nomoto F , Miura H , Takahashi Y , Fujita N
Ref : DNA Research , 17 :393 , 2010
Abstract : Kitasatospora setae NBRC 14216(T) (=KM-6054(T)) is known to produce setamycin (bafilomycin B1) possessing antitrichomonal activity. The genus Kitasatospora is morphologically similar to the genus Streptomyces, although they are distinguishable from each other on the basis of cell wall composition and the 16S rDNA sequence. We have determined the complete genome sequence of K. setae NBRC 14216(T) as the first Streptomycetaceae genome other than Streptomyces. The genome is a single linear chromosome of 8,783,278 bp with terminal inverted repeats of 127,148 bp, predicted to encode 7569 protein-coding genes, 9 rRNA operons, 1 tmRNA and 74 tRNA genes. Although these features resemble those of Streptomyces, genome-wide comparison of orthologous genes between K. setae and Streptomyces revealed smaller extent of synteny. Multilocus phylogenetic analysis based on amino acid sequences unequivocally placed K. setae outside the Streptomyces genus. Although many of the genes related to morphological differentiation identified in Streptomyces were highly conserved in K. setae, there were some differences such as the apparent absence of the AmfS (SapB) class of surfactant protein and differences in the copy number and variation of paralogous components involved in cell wall synthesis.
ESTHER : Ichikawa_2010_DNA.Res_17_393
PubMedSearch : Ichikawa_2010_DNA.Res_17_393
PubMedID: 21059706
Gene_locus related to this paper: kitsk-e4n1a1 , kitsk-e4n2t9 , kitsk-e4n4j8 , kitsk-e4n6l6 , kitsk-e4n9v4 , kitsk-e4n533 , kitsk-e4n648 , kitsk-e4na97 , kitsk-e4nas1 , kitsk-e4nas4 , kitsk-e4nf33 , kitsk-e4ngi3 , kitsk-e4nj77 , kitsk-e4ngr7 , kitsk-e4n1n8 , kitsk-e4n5j9 , kitsk-e4ndj5 , kitsk-e4ni45 , kitsk-e4nik2