PolyAspartate-hydrolase

Relationship

Family: PolyAspartate-hydrolase

Block: X

Parent Family: Abhydrolase_5

Comment

Poly(aspartate) (PAA) is a bio-based, biocompatible, biodegradable alternative to polycarboxylate of poly(acrylate). Bacterial PAA-hydrolyzing enzyme can also perform synthesis of poly(alpha-ethyl beta-aspartate). This family is close to PHB depolymerase. The LpqC, poly(3-hydroxybutyrate) depolymerase from Bordetella parapertussis (CASP Target) (structure 3D0K) belongs to this family. Polyaspartic acid (PASA) is also a natural polymer as fragment of larger proteins with length up to 50 amino acids. Synthetic tPAA(thermally synthesized PAA) consists of beta-amide (70%) and alpha-amide,(30%) D- and L-aspartate units; the alpha- and beta-amide units are randomly distributed. PAA hydrolase-1 is an alpha beta hydrolase inhibited by PMSF and DFP. PAA hydrolase-2 is closer to metallo carboxypeptidase inhibited by DFP and PMSF

Database

Interpro : No interpro

PIRSF : No PIRSF

Pdoc : No Pdoc

Pfam : PF12695 Abhydrolase_5

Prints : No Print

EC Number : No EC Number

Sequences

Peptide in Fasta
Nucleotide in Fasta
Alignment with Multalin Text only
Seed alignment with MAFFT No colour
Alignment with MAFFT No colour
Dendrogram The dnd file

References (3)

Title : Poly(aspartate) hydrolases: biochemical properties and applications - Hiraishi_2011_Appl.Microbiol.Biotechnol_91_895
Author(s) : Hiraishi T , Maeda M
Ref : Applied Microbiology & Biotechnology , 91 :895 , 2011
Abstract : Hiraishi_2011_Appl.Microbiol.Biotechnol_91_895
ESTHER : Hiraishi_2011_Appl.Microbiol.Biotechnol_91_895
PubMedSearch : Hiraishi_2011_Appl.Microbiol.Biotechnol_91_895
PubMedID: 21713512

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 : Hiraishi_2009_Macromol.Biosci_9_10
ESTHER : Hiraishi_2009_Macromol.Biosci_9_10
PubMedSearch : Hiraishi_2009_Macromol.Biosci_9_10
PubMedID: 18756460
Gene_locus related to this paper: 9sphi-b6vqa9

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 : Hiraishi_2003_Biomacromolecules_4_80
ESTHER : Hiraishi_2003_Biomacromolecules_4_80
PubMedSearch : Hiraishi_2003_Biomacromolecules_4_80
PubMedID: 12523851
Gene_locus related to this paper: 9sphn-q7wsc1

Structures (3)

Genes Proteins in PolyAspartate-hydrolase family (56)

No fragment of genes

Structures in PolyAspartate-hydrolase family (3)

Substrates in PolyAspartate-hydrolase family (2)

Inhibitors in PolyAspartate-hydrolase family (2)