Kajiyama M

References (2)

Title : Genetic Analysis and Characterization of Poly(aspartic acid) Hydrolase-1 from Sphingomonas sp. KT-1 - Hiraishi_2003_Biomacromolecules_4_80
Author(s) : Hiraishi T , Kajiyama M , Tabata K , Yamato I , Doi Y
Ref : Biomacromolecules , 4 :80 , 2003
Abstract : Sphingomonas sp. KT-1 hydrolyzes poly(aspartic acid) (PAA) containing alpha- and beta-amide units and has at least two different types of PAA hydrolases. The PAA hydrolase-1 hydrolyzes selectively beta-beta amide units in PAA. Molecular cloning of PAA hydrolase-1 from Sphingomonas sp. KT-1 has been carried out to characterize its gene products. Genetic analysis shows that the deduced amino acid sequence of PAA hydrolase-1 has a similarity with those of the catalytic domain of poly(3-hydroxybutyric acid) (PHB) depolymerases from Alcaligenes faecalis AE122 and Pseudomonas lemoignei. Site-specific mutation analysis indicates that (176)Ser is a part of a strictly conserved pentapeptide sequence (Gly-Xaa-Ser-Xaa-Gly), which is the lipase box, and plays as an active residue.
ESTHER : Hiraishi_2003_Biomacromolecules_4_80
PubMedSearch : Hiraishi_2003_Biomacromolecules_4_80
PubMedID: 12523851
Gene_locus related to this paper: 9sphn-q7wsc1

Title : Purification and characterization of poly(aspartic acid) hydrolase from Sphingomonas sp. KT-1 - Tabata_2001_Biomacromolecules_2_1155
Author(s) : Tabata K , Kajiyama M , Hiraishi T , Abe H , Yamato I , Doi Y
Ref : Biomacromolecules , 2 :1155 , 2001
Abstract : Poly(aspartic acid) (PAA) hydrolase was purified from Sphingomonas sp. KT-1 (JCM10459). The purified hydrolase degraded thermally synthesized PAA to oligomers. The molecular mass of PAA hydrolase was 30 kDa and the isoelectric point was 8.9. The optimum values of pH and temperature for PAA degradation were 10.0 and 40 degrees C, respectively. The investigation of the effect of inhibitors for the PAA-degrading activities has revealed that the PAA hydrolase is a serine-type hydrolase. The structural analysis of PAA-degraded products using (1)H and (13)C nuclear magnetic resonances has indicated that the purified enzyme hydrolyzes selectively the beta-amide linkage connecting with beta-aspartic acid units in PAA.
ESTHER : Tabata_2001_Biomacromolecules_2_1155
PubMedSearch : Tabata_2001_Biomacromolecules_2_1155
PubMedID: 11777387