(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 > asterids: NE > lamiids: NE > Solanales: NE > Solanaceae: NE > Solanoideae: NE > Solaneae: NE > Solanum: NE > Lycopersicon: NE > Solanum pennellii: NE
Warning: This entry is a compilation of different species or line or strain with more than 90% amino acide identity. You can retrieve all strain data
(Below N is a link to NCBI taxonomic web page and E link to ESTHER at designed phylum.) Solanum pennellii: N, E.
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 MARVTLFLLLLLVYGVVSEHFIVETLPGFHGKLPFTLETGYISVGEEEKV QLFYFFVQSERDPRNDPLMIWLTGGPGCSGLSSFVYEIGPLTFDYANSSG NFPKLELNSYSWTKVANIIFIDQPAGTGYSYANTSEAYNCNDTLSVTLTY DFLRKWLMDHPEYLNNPLYVGGDSYSGIFVALLTRKIYDGIEVGDRPRVN IKGYIQGNALTDRSIDFNGRVKYANHMGLISDKIYQSAKANCNGNYIDVD PNNILCLNDLQKVTRCLKNIRRAQILEPYCDLPYLMGILQETPTNGQSVF PIAGPWCREKNYIYSYVWANDKAVQKALNVREGTTLEWVRCNESMHYRGK ERTESYVYDVPSVIDDHQHLTSKSCRALIYSGDHDMVVPHLSTEEWIETL KLPIADDWEPWFVDDQVAGYKVKYLQNDYEMTYATVKGAGHTAPEYKPEQ CLPMVDRWFSGDPL
References
Title: An acyltransferase catalyzing the formation of diacylglucose is a serine carboxypeptidase-like protein Li AX, Steffens JC Ref: Proc Natl Acad Sci U S A, 97:6902, 2000 : PubMed
1-O-beta-acyl acetals serve as activated donors in group transfer reactions involved in plant natural product biosynthesis and hormone metabolism. However, the acyltransferases that mediate transacylation from 1-O-beta-acyl acetals have not been identified. We report the identification of a cDNA encoding a 1-O-beta-acylglucose-dependent acyltransferase functioning in glucose polyester biosynthesis by Lycopersicon pennellii. The acyltransferase cDNA encodes a serine carboxypeptidase-like protein, with a conserved Ser-His-Asp catalytic triad. Expression of the acyltransferase cDNA in Saccharomyces cerevisiae conferred the ability to disproportionate 1-O-beta-acylglucose to diacylglucose. The disproportionation reaction is regiospecific, catalyzing the conversion of two equivalents of 1-O-beta-acylglucose to 1, 2-di-O-acylglucose and glucose. Diisopropyl fluorophosphate, a transition-state analog inhibitor of serine carboxypeptidases, inhibited acyltransferase activity and covalently labeled the purified acyltransferase, suggesting the involvement of an active serine in the mechanism of the transacylation. The acyltransferase exhibits no carboxypeptidase activity; conversely, the serine carboxypeptidases we have tested show no ability to transacylate using 1-O-acyl-beta-glucoses. This acyltransferase may represent one member of a broader class of enzymes recruited from proteases that have adapted a common catalytic mechanism of catabolism and modified it to accommodate a wide range of group transfer reactions used in biosynthetic reactions of secondary metabolism. The abundance of serine carboxypeptidase-like proteins in plants suggests that this motif has been used widely for metabolic functions.
Title: Glucose polyester biosynthesis. Purification and characterization of a glucose acyltransferase Li AX, Eannetta N, Ghangas GS, Steffens JC Ref: Plant Physiol, 121:453, 1999 : PubMed
Glandular trichomes of the wild tomato species Lycopersicon pennellii secrete 2,3,4-O-tri-acyl-glucose (-Glc), which contributes to insect resistance. A Glc acyltransferase catalyzes the formation of diacyl-Glc by disproportionating two equivalents of 1-O-acyl-beta-Glc, a high-energy molecule formed by a UDP-Glc dependent reaction. The acyltransferase was purified 4,900-fold from L. pennellii leaves by polyethylene glycol fractionation, diethylaminoethyl chromatography, concanavalin A affinity chromatography, and chromatofocusing. The acyltransferase possesses an isoelectric point of 4.8, a relative molecular mass around 110 kD, and is composed of 34- and 24-kD polypeptides as a heterotetramer. The 34- and 24-kD proteins were partially sequenced. The purified enzyme catalyzes both the disproportionation of 1-O-acyl-beta-Glcs to generate 1,2-di-O-acyl-beta-Glc and anomeric acyl exchange between 1-O-acyl-beta-Glc and Glc.
