| 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. |
| PubMedSearch : Hiraishi_2003_Biomacromolecules_4_80 |
| PubMedID: 12523851 |
| Gene_locus related to this paper: 9sphn-q7wsc1 |
| Substrate | Polyaspartic-acid |
| Gene_locus | 9sphn-q7wsc1 |
| Family | PolyAspartate-hydrolase |
Hiraishi T, Kajiyama M, Tabata K, Yamato I, Doi Y (2003)
Genetic Analysis and Characterization of Poly(aspartic acid) Hydrolase-1 from Sphingomonas sp. KT-1
Biomacromolecules
4 :80
Hiraishi T, Kajiyama M, Tabata K, Yamato I, Doi Y (2003)
Biomacromolecules
4 :80