| Title : Cloning of poly(aspartic acid) (PAA) hydrolase-1 gene from Pedobacter sp. KP-2 and hydrolysis of thermally synthesized PAA by its gene product - Hiraishi_2009_Macromol.Biosci_9_10 |
| Author(s) : Hiraishi T , Masuda E , Kanayama N , Nagata M , Doi Y , Abe H , Maeda M |
| Ref : Macromol Biosci , 9 :10 , 2009 |
|
Abstract :
Pedobacter sp. KP-2 can degrade and metabolize thermally synthesized alpha,beta-poly(D,L-aspartic acid) (tPAA), which contains 70% of unnatural beta-amide units, with high-molecular-weight. In this study, gene cloning and molecular characterization of PAA hydrolase-1 from KP-2 was carried out. Gene analysis reveals that deduced amino acid sequence of the enzyme shows a similarity to only that of PAA hydrolase-1 from Sphingomonas sp. KT-1. GPC and NMR analyses of the hydrolyzed products of tPAA by PAA hydrolase-1 of KP-2 indicate that this enzyme cleaves the beta-beta amide linkage via endo-mode to yield oligo(aspartic acid) from tPAA. Taking the composition of tPAA and the substrate specificity of PAA hydrolase-1 into consideration, the enzyme possibly plays a crucial role in tPAA biodegradation by KP-2. |
| PubMedSearch : Hiraishi_2009_Macromol.Biosci_9_10 |
| PubMedID: 18756460 |
| Gene_locus related to this paper: 9sphi-b6vqa9 |
| Substrate | Polyaspartic-acid |
| Gene_locus | 9sphi-b6vqa9 |
| Family | PolyAspartate-hydrolase |
Hiraishi T, Masuda E, Kanayama N, Nagata M, Doi Y, Abe H, Maeda M (2009)
Cloning of poly(aspartic acid) (PAA) hydrolase-1 gene from Pedobacter sp. KP-2 and hydrolysis of thermally synthesized PAA by its gene product
Macromol Biosci
9 :10
Hiraishi T, Masuda E, Kanayama N, Nagata M, Doi Y, Abe H, Maeda M (2009)
Macromol Biosci
9 :10