(Below N is a link to NCBI taxonomic web page and E link to ESTHER at designed phylum.) > cellular organisms: NE > Eukaryota: NE > Viridiplantae: NE > Streptophyta: NE > Streptophytina: NE > Embryophyta: NE > Tracheophyta: NE > Euphyllophyta: NE > Spermatophyta: NE > Magnoliophyta: NE > Mesangiospermae: NE > eudicotyledons: NE > Gunneridae: NE > Pentapetalae: NE > rosids: NE > malvids: NE > Brassicales: NE > Brassicaceae: NE > Brassiceae: NE > Raphanus: NE > Raphanus sativus: NE
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 MSSSESPPQEKITAPYGSWKSPITADVVSGASKRLGGTAVDSRGRLVWLE SRPNESGREVLVMEGEKEGGIDITPKEFGVRTLTQEYGGGAFRVSSSHDQ LVVFSNYKDQRLYKQHFANKDSSPKPITPDYGSPAVTYADGVFDSRFNRF VTVREDGRLDRSNPITTIVEVNLSGGDTLEEPKVLVSGNDFYAFPRLDPK CERLAWIQWTLPNMPWDKAQLWVGYISESGTIDKRVCVAGCDPEYVESPT EPKWSPRGELFFVTDRKNGFWNIHKWIESTNEVVSVYPLDGEFTKPLWVF GTNSYEIIECSEEKNLIACSYRQKGKSYLGILDDSKGSCSLLDIPLTDFD NITLGNQCLYVEGASAVLPPSVAKVTLDKHKMKALSSEIVWSSSTDVLKY KSFFSAPDLIEFPTEVPGQNAYAYFYPPTNPLYNASIEEKPPLIVKSHGG PSAESRGSLNLIIQYWTSRGWAFVDVNYGGSTGYGREYRERVLRRWGIVD VDDCCGCAKYLVSSGKADVKRLFISGGSAGGYTALTALALRDVFKAGASL YGVADLKMLKEGHKFESRYIDSLVEEEKDFYERSPINFVDRFSCPIILFQ GLEDKIVNPDQTRKIYQALKEKGVPVALVEYEGEEHGFRKAENIKYTLEQ LMVFFARVVGGFQVADDITPLKIDNFDTSSDA
Reference
Title: Identification of a plant aminopeptidase with preference for aromatic amino acid residues as a novel member of the prolyl oligopeptidase family of serine proteases Tsuji A, Fujisawa Y, Mino T, Yuasa K Ref: J Biochem, 150:525, 2011 : PubMed
Genome analysis has indicated that plants, like animals, possess a variety of protease genes. However, bulk of putative proteases has not been characterized at the enzyme level. In this article, a novel enzyme that hydrolyses phenylalanyl-4-methylcoumaryl 7-amide (phenylalanyl-MCA) was purified from cotyledons of daikon radish by ammonium sulphate fractionation and successive chromatography with DEAE-cellulose, phenyl-Sepharose, Sephacryl S-200 and Mini-Q. The molecular mass of the enzyme was estimated to be 78 kDa by SDS-PAGE under reducing conditions and 74 kDa by gel filtration, indicating that the enzyme is a monomer. The deduced amino acid sequence from the cDNA nucleotide sequence indicated that the enzyme is an orthologue of Arabidopsis unidentified protein, acylpeptide hydrolase-like protein (AHLP; UniProt ID: Q9FG66) belonging to the prolyl oligopeptidase (POP) family of a serine-type peptidase predicted from genetic information. Good substrates identified for the enzyme include phenylalanyl-MCA, tyrosyl-MCA and enkephalin. Neither acylamino acid-releasing activity nor endopeptidase activity was detected. The enzyme cleaved enkephalin (YGGFM, YGGFL), whereas, BAM-12 P (YGGFMRRVGRPE) and dynorphin A (YGGFLRRIRPKLK) were not digested. These results suggested that the enzyme possesses strict size selectivity of substrate. We propose the name 'tyrosyl aminopeptidase' for the uncharacterized protein AHLP.
