(Below N is a link to NCBI taxonomic web page and E link to ESTHER at designed phylum.) > cellular organisms: NE > Bacteria: NE > Proteobacteria: NE > Gammaproteobacteria: NE > Cellvibrionales: NE > Microbulbiferaceae: NE > Microbulbifer: NE > Microbulbifer arenaceous: NE
Molecular evidence
Database
No mutation 3 structures: 7VGB, 7VGC, 7Y1X 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 MRKPAIALVAACAAVAAIAVTRGTDTQSSHNYPDTATVDQQDDYFGTAVT DPYRWLEQQDSKLVKDWVTAQNDFSLPTLKALPHWQKINDRLTELWQYER YGVPYKKAGQVFYEYNDGSWDQSVFYRTADIHKDGHVILDPRALSKDGTI AAKRYTVSPNGRYLAYGTSDGGTDWTDYRVRDLKTRRMIPDHLTGIKFSD ASWAKDESGFYYSRYPFKEDGSADDSKQVSVYFHKIGEPQSKDQLIYKIT DHPTRNPGAQVSDDGKYLILGVFDGYDSNGIYYKDLQDGESRVVKLLDDW DALYTYLGNQGKTFYFETNVDATNGRIIAIDIDKPQKDHWKILVPEQKDA LQSASLIGGRFVLHYLEDAKSKVVVTDLDGKQQYALKLPGMGTVEGFTGD PDDPETYYAFSNFLTPPSIYKLNVHSGNSEIVKSPKYPADFSDYVVSQEF FTSKDGTRVPLFLVHKKGLKKYGKNPTLLYGYGGFNAAQLPRFYTRFAGW LDMGGTFAMVNLRGGSEYGGAWHKAGTKLQKQNVFDDFIGAAEWLIEEKI TSPEKLGIMGRSNGGLLVGATEVQRPELFAVALPIVGVLDMLRYHTASAN ARQWSSDYGLSENKAEFNALYAYSPVHNTKKGTCYPATLITTADRDDRVV PWHSYKFAASLQRDQGCDNPIYLAVETRAGHGAGKPVWMQVEDFTNQYAF LADQLGLQVEK
Reference
Title: The structure and molecular dynamics of prolyl oligopeptidase from Microbulbifer arenaceous provide insights into catalytic and regulatory mechanisms Huang, P, Lv A, Yan Q, Jiang Z, Yang S. Ref: Acta Crystallographica D Biol Crystallogr, 78:735, 2022 : PubMed
Prolyl oligopeptidases (POPs) are atypical serine proteases that are unique in their involvement in the maturation and degradation of prolyl-containing peptide hormones and neuropeptides. They are potential pharmaceutical targets for the treatment of several neurodegenerative disorders, such as Alzheimer's disease. In this study, the catalytic and substrate-regulatory mechanisms of a novel bacterial POP from Microbulbifer arenaceous (MaPOP) were investigated. The crystal structure revealed that the catalytic triad of MaPOP was covered by the central tunnel of an unusual beta-propeller domain. The tunnel not only provided the sole access to the active site for oligopeptides, but also protected large structured peptides or proteins from accidental proteolysis. The enzyme was able to cleave angiotensin I specifically at the carboxyl side of the internal proline residue, but could not hydrolyze long-chain bovine insulin B in vitro. Like the ligand-free structure, MaPOP bound to the transition-state analog inhibitor ZPR was also in a closed state, which was not modulated by the common `latching loop' found in other POPs. The substrate-assisted catalytic mechanism of MaPOP reported here may represent a common mechanism for all POPs. These results may facilitate a better understanding of the catalytic behavior of POPs under physiological conditions.
Microbulbifer arenaceous prolyl oligopeptidase MaPOP
