(Below N is a link to NCBI taxonomic web page and E link to ESTHER at designed phylum.) > cellular organisms: NE > Bacteria: NE > Terrabacteria group: NE > Firmicutes: NE > Bacilli: NE > Bacillales: NE > Alicyclobacillaceae: NE > Alicyclobacillus: NE > Alicyclobacillus tengchongensis: 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 MHMPMIDLPYEELLNYRGRNPRPSDFDAYWERGLAEMKEVDAKLEIVPNS FSTSQVECFDLYFTGVKGARIHSLYARPRHATAPHPAILQFHGYKGHAGD WLDKMAYAAHGFTVVAMNCRGQGGHSQDTHPVRGMTSSGHVVRGLDDHPD NLYFRQVFLDTAQLANIVMNLPEVDPDLVAVTGWSQGGALTVACAALEPR IRRAAPVYPFLSDYLRVWEMDFGGVHEELIQYFRNRDPLHANRDLIFEKL GYIDIQHLADRINAEVLWGIGLMDKVCPPSTQFAAYNRIRSPKRMVVYPD FQHEWLPGMNDAIFEWMLTM
Reference
Title: Characterization of EstZY: A new acetylesterase with 7-aminocephalosporanic acid deacetylase activity from Alicyclobacillus tengchongensis Ding J, Zhou Y, Zhu H, Deng M, Gao Y, Yang Y, Huang Z Ref: Int J Biol Macromol, 148:333, 2020 : PubMed
Deacetyl-7-aminocephalosporanic acid (D-7-ACA) is required for producing of many semisynthetic beta-lactam antibiotics; therefore, enzymes capable of converting 7-aminocephalosporanic acid (7-ACA) to D-7-ACA present a valuable resource to the pharmaceutical industry. In the present study, a putative acetylesterase, EstZY, was identified and characterized from a thermophilic bacterium Alicyclobacillus tengchongensis. Sequence alignment showed that EstZY was an acetylesterase which belonged to carbohydrate esterase family 7 (CE7), with substrate preference for short-chain acyl esters p-NPC(2) to p-NPC(8). Maximum enzyme activity was recorded at pH 9.0 and 50 degreesC, where K(m) and V(max) were calculated as 1.9 +/- 0.23 mM and 258 +/- 18.5 microM min(-)(1), respectively. The residues Ser185, Asp274, and His303 were identified as the putative catalytic triad by homology modelling, site-directed mutagenesis and molecular docking. Moreover, EstZY can remove the acetyl group at C3' position of 7-ACA to form D-7-ACA; this is the first report of a 7-ACA deacetylase from CE7 family in A. tengchongensis and may represent a new enzyme with industrial values.
