(Below N is a link to NCBI taxonomic web page and E link to ESTHER at designed phylum.) > cellular organisms: NE > Bacteria: NE > FCB group: NE > Bacteroidetes/Chlorobi group: NE > Bacteroidetes: NE > Sphingobacteriia: NE > Sphingobacteriales: NE > Sphingobacteriaceae: NE > Pedobacter: NE > Pedobacter sp. KP-2: NE
Molecular evidence
Database
No mutation 1 structure: 8DNB: WITHDRAWN Expanding structural knowledge of poly(aspartic acid) hydrolases: Structure determination of Pedobacter sp. KP-2 PahZ1 No kinetic
LegendThis sequence has been compared to family alignement (MSA) red => minority aminoacid blue => majority aminoacid color intensity => conservation rate title => sequence position(MSA position)aminoacid rate Catalytic site Catalytic site in the MSA MITTKHLTTIAAFCLIVMANSVCEAHKAHKQPHRQTINPKIDEGVGEFIY QDYKPLDNKPIKVRYYNPGKNDAQVLFIMHGNGRNAEGYFKAMLKHAQQH NVLLVVPEFDEQQFSSREYHQGGILDKQSKLRPREDWTFSIIEPLFDYVK KLTGNTSAGYMLYGFSAGSQFVHRFLMFNPENRVTRAIAGSAGTYTMPDY NIDYSYGLKNVNLPQKNLNKFFAKNLMVIVGDADTVLSRTDLVKTPAANQ QGRDRVERGQTFFNRSKAIAEQLKTPFNWKFQLIPHVGHSQGEMAGPVAK LLFEDK
Reference
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 T, Masuda E, Kanayama N, Nagata M, Doi Y, Abe H, Maeda M Ref: Macromol Biosci, 9:10, 2009 : PubMed
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.
Pedobacter sp. KP-2 Poly(Aspartic acid) hydrolase-1
