The enzyme, characterized from pollen of the plant Tulipa gesneriana (tulip), catalyses the intramolecular transesterification of 6-tuliposide B to form the antibiotic aglycon tulipalin B as a sole product. It does not catalyse the hydrolysis of 6-tuliposide B to form a hydroxy acid. The enzyme has marginal activity with 6-tuliposide A. cf. EC 4.2.99.22, tuliposide A-converting enzyme.
putative reaction mechanism of TCE enzymes, overview. The reaction begins with a nucleophilic attack by the catalytic Ser, whose hydroxyl group is activated by the charge relay of the catalytic triad, on the carbonyl carbon of 6-Pos. This is followed by the formation of a tetrahedral intermediate, which is stabilized by the oxyanion hole structure contributed by the two Gly residues of the HGG motif. Then, following the elimination of glucose, the acyl-enzyme complex is formed, and an intramolecular nucleophilic attack by a terminal hydroxyl group of 6-Pos, but not by water, occurs. This nucleophilic attack results in the formation of the five-membered ring structure of Pa. If the acylenzyme complex is subjected to a nucleophilic attack by activated water, then ?-hydroxy acids are released as hydrolytic products, but this process never occurs in the TCE reactions
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SYSTEMATIC NAME
IUBMB Comments
6-tuliposide B D-glucose-lyase (tulipalin B-forming)
The enzyme, characterized from pollen of the plant Tulipa gesneriana (tulip), catalyses the intramolecular transesterification of 6-tuliposide B to form the antibiotic aglycon tulipalin B as a sole product. It does not catalyse the hydrolysis of 6-tuliposide B to form a hydroxy acid. The enzyme has marginal activity with 6-tuliposide A. cf. EC 4.2.99.22, tuliposide A-converting enzyme.
i.e. PosD, the enzyme catalyzes intramolecular transesterification, PosD is a 1,6-diacyl-glucose type of Pos, the enzyme shows 4.3% activity with PosD compared to 6-PosB
i.e. 6-PosA, a monoacyl-glucose type of Pos, the enzyme catalyzes intramolecular transesterification, the enzyme shows 0.72% activity with 6-PosA compared to 6-PosB
i.e. PosF, the enzyme catalyzes intramolecular transesterification, PosF is a 1,6-diacyl-glucose type of Pos, the enzyme shows 59% activity with PosF compared to 6-PosB, the configuration at the C-3' position of the substrate PosF is S-form
TCE enzymes are lactone-forming enzymes and a non-ester-hydrolyzing carboxylesterase, and specifically catalyze intramolecular transesterification, but not hydrolysis
6-PosB is chemically labile, and they can be spontaneously converted to PaB in neutral to weakly basic conditions in vitro. 1-Tuliposide A (1-PosA) is no substrate
enzme TCEB preferentially catalyzes the conversion of 6-PosB to PaB, and catalyzes intramolecular transesterification of 6-tuliposide B (6-PosB) to form tulipalins B (PaB), but neither the hydrolysis of 6-Pos nor Pa. 1alpha- and 1beta-anomers exist for 6-PosB, and both anomers serve as substrates for TCEB. All three TCEB isoforms preferentially catalyze the conversion of 6-PosB to PaB, with about 0.4-2% activities toward 6-PosA
TCE enzymes are lactone-forming enzymes and a non-ester-hydrolyzing carboxylesterase, and specifically catalyze intramolecular transesterification, but not hydrolysis
Report From the International Society of Urological Pathology (ISUP) Consultation Conference on Molecular Pathology of Urogenital Cancers: III: Molecular Pathology of Kidney Cancer.
Renal Cell Carcinoma With Leiomyomatous Stroma: A Group of Tumors With Indistinguishable Histopathologic Features, But 2 Distinct Genetic Profiles: Next-Generation Sequencing Analysis of 6 Cases Negative for Aberrations Related to the VHL gene.
A 12-gene expression signature is associated with aggressive histological in prostate cancer: SEC14L1 and TCEB1 genes are potential markers of progression.
TCE enzymes belong to the carboxylesterase family in the alpha/beta-hydrolase fold superfamily, and specifically catalyze intramolecular transesterification, but not hydrolysis, functional diversity of carboxylesterases and related alpha/beta-hydrolase enzymes and proteins in plants, overview. TgTCEA1 and TgTCEB1 polypeptides show 52% identity to each other and approximately 40-45% identities to the sequences annotated as plant carboxylesterases. TgTCEs catalyze only intramolecular transesterification, while other plant carboxylesterases catalyze the hydrolysis of carboxylic esters to form carboxylic acids and alcohols. TgTCE polypeptides have sequence motifs typical of class I carboxylesterases in the alpha/beta-hydrolase fold superfamily, including the HGG motif. The two Gly residues in this motif are involved in the formation of an oxyanion hole structure during the formation of the acyl-enzyme complex. The other conserved motif is the catalytic triad Ser, Asp, and His, of which the catalytic Ser is present within the conserved pentapeptide sequence Gly-X-Ser-X-Gly
tuliposide A converting enzyme (TCEA) and tuliposide B-converting enzyme (TCEB) catalyze intramolecular transesterification of 6-PosA and 6-PosB to form the corresponding lactones, PaA and PaB, respectively, and D-glucose. 6-PosA and 6-PosB serve as precursors of the corresponding alpha-methylene-gamma-butyrolactones, tulipalins A (PaA) and B (PaB), respectively, which are formed from the acyl group at the C-6 position. The 1alpha- and 1beta-anomers exist for 6-PosA/6-PosB and both anomers serve as substrates for TCEs. TCEA and TCEB catalyze the formation of PaA/1-PosA and PaB/1-PosA from PosD and PosF, respectively, by acting on the 6-acyl group of PosD and PosF. Neither enzyme acts on the 1-acyl group of PosD, PosF, or 1-PosA. Although intact tulip tissues constitutively accumulate large amounts of 6-Pos, biologically active PaA and PaB are far less abundant and are sometimes barely detectable, PaA and PaB are hardly detectable in intact plants. PaA and PaB respectively show antifungal and antibacterial activities, they are considered to be key secondary metabolites in the chemical defense of tulip, while 6-PosA and 6-PosB are considered to be storage forms of PaA and PaB, respectively. Enzyme TCEB shows lower overall activity than enzyme TCEA
tuliposides (Pos) and tulipalins (Pa) are the major defensive secondary metabolites in tulip (Tulipa gesneriana). So far, seven analogues of Pos have been reported: 1-PosA, 1-PosB, 6-PosA, 6-PosB, PosD, PosE, and PosF, which differ in the number, position, and structure of the acyl side chain. They are categorized into monoacyl-glucose type (1-Pos and 6-Pos) and 1,6-diacyl-glucose type (PosD, PosE, and PosF), overview. The tuliposide-converting enzyme (TCE), a non-ester-hydrolyzing carboxylesterase, catalyzes the conversion of major defensive secondary metabolites, tuliposides, to antimicrobial tulipalins. PaA has been shown to have potent insecticidal activity against several insect pests, such as Thrips palmi. PaA functions as an antifungal agent rather than an antibacterial agent, and vice versa for PaB. Enzyme-mediated activation of postinhibitins
comparison of the full-length TgTCE polypeptides with the N-termini of the corresponding native TCEs purified from tulip tissues indicated that the enzymes are translated as precursor polypeptides before being processed to mature polypeptides via cleavage of the N-terminal transit peptides
gene TgTCEB1, sequence comparisons and unrooted phylogenetic tree, functional recombinant expression of the mature dimeric enzyme in Escherichia coli. Although the recombinant enzyme is functionally expressed as N-terminal His-tagged protein, removal of the vector-derived sequence including His-tag by protease treatment almost doubles its activity, allowing for accurate assessment of enzyme characteristics. Recombinant transient expression of GFP-tagged N-terminal transit peptides of TCEB in onion epidermal cell plastids
PaA and PaB are considered to be useful natural products with potential applications as synthetic intermediates in the production of several bioactive compounds, antimutagenic agents, insect repellents, and as monomers of functional biobased polymers, application of TCE to produce PaB, overview