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Information on EC 4.2.99.23 - tuliposide B-converting enzyme
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4.2.99.23 tuliposide B-converting enzymeIUBMB Comments
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.
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Word Map
The expected taxonomic range for this enzyme is: Tulipa gesneriana
Synonyms
tceb1, tgtceb1, posb-converting enzyme, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
PosB-converting enzyme
TCEB
tuliposide-converting enzyme
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
6-tuliposide B = tulipalin B + D-glucose
-
-
-
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6-tuliposide B = tulipalin B + D-glucose
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.
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
1,6-tuliposide D
tulipalin A + 1-tuliposide A
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
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-
?
6-tuliposide A
tulipalin A + D-glucose
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the activities of isoforms 1, 2 and 3 towards 6-tuliposide A are 0.41, 1.8, and 1.8% of those towards P6-tuliposide B, respectively
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-
?
6-tuliposide A
tulipalin A + D-glucose
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
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-
?
6-tuliposide A
tulipalin A + D-glucose
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i.e. 6-PosA, enzyme TCEB shows 0.4-2.0% activity with 6-PosA compared to 6-PosB
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-
?
6-tuliposide B
tulipalin B + D-glucose
i.e. 6-PosB, a monoacyl-glucose type of Pos, the enzyme catalyzes intramolecular transesterification, best substrate
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?
6-tuliposide B
tulipalin B + D-glucose
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i.e. 6-PosB, preferred substrate
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-
?
tuliposide F
(3R)-3-hydroxy-2-methylidenecyclopentan-1-one + 1-tuliposide A
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-
?
tuliposide F
(3R)-3-hydroxy-2-methylidenecyclopentan-1-one + 1-tuliposide A
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
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-
?
additional information
?
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-
TCE enzymes are lactone-forming enzymes and a non-ester-hydrolyzing carboxylesterase, and specifically catalyze intramolecular transesterification, but not hydrolysis
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?
additional information
?
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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
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-
?
additional information
?
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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
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?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
tuliposide F
(3R)-3-hydroxy-2-methylidenecyclopentan-1-one + 1-tuliposide A
-
-
-
?
additional information
?
-
-
TCE enzymes are lactone-forming enzymes and a non-ester-hydrolyzing carboxylesterase, and specifically catalyze intramolecular transesterification, but not hydrolysis
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-
?
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
phenylmethylsulfonyl fluoride
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2 mM inhibits the activity of isoforms 1, 2 and 3 by 89, 99.7 and 90.2%, respectively
phenylmethylsulfonyl fluoride
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remarkably reduces the activity of the native enzyme purified from tulip
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Breast Neoplasms
Amplification of 8q21 in breast cancer is independent of MYC and associated with poor patient outcome.
Carcinoma
Antitumor effect and biological pathways of a recombinant adeno-associated virus as a human renal cell carcinoma suppressor.
Carcinoma
Renal cell carcinomas with a mesenchymal stromal component: what do we know so far?
Carcinoma
Renal cell tumors with clear cell histology and intact VHL and chromosome 3p: a histological review of tumors from the Cancer Genome Atlas database.
Carcinoma
TCEB1-mutated renal cell carcinoma: a distinct genomic and morphological subtype.
Carcinoma, Renal Cell
Antitumor effect and biological pathways of a recombinant adeno-associated virus as a human renal cell carcinoma suppressor.
Carcinoma, Renal Cell
Renal cell carcinomas with a mesenchymal stromal component: what do we know so far?
Carcinoma, Renal Cell
Renal cell tumors with clear cell histology and intact VHL and chromosome 3p: a histological review of tumors from the Cancer Genome Atlas database.
Carcinoma, Renal Cell
TCEB1-mutated renal cell carcinoma: a distinct genomic and morphological subtype.
Kidney Neoplasms
Clear cell renal cell carcinoma with wild-type von Hippel-Lindau gene: a non-existent or new tumour entity?
Kidney Neoplasms
Report From the International Society of Urological Pathology (ISUP) Consultation Conference on Molecular Pathology of Urogenital Cancers: III: Molecular Pathology of Kidney Cancer.
Neoplasm Metastasis
NF-?B-activated SPRY4-IT1 promotes cancer cell metastasis by downregulating TCEB1 mRNA via Staufen1-mediated mRNA decay.
Neoplasms
Clear cell renal cell carcinoma with wild-type von Hippel-Lindau gene: a non-existent or new tumour entity?
Neoplasms
NF-?B-activated SPRY4-IT1 promotes cancer cell metastasis by downregulating TCEB1 mRNA via Staufen1-mediated mRNA decay.
Neoplasms
Putative Drivers of Aggressiveness in TCEB1-mutant Renal Cell Carcinoma: An Emerging Entity with Variable Clinical Course.
Neoplasms
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.
Neoplasms
Renal cell carcinoma with leiomyomatous stroma: a review of an emerging entity distinct from clear cell conventional renal cell carcinoma.
Neoplasms
TCEB1-mutated renal cell carcinoma: a distinct genomic and morphological subtype.
Prostatic Neoplasms
A 12-gene expression signature is associated with aggressive histological in prostate cancer: SEC14L1 and TCEB1 genes are potential markers of progression.
Tuberous Sclerosis
Renal cell carcinoma with leiomyomatous stroma: a review of an emerging entity distinct from clear cell conventional renal cell carcinoma.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
Michaelis-Menten kinetics
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1.3
6-tuliposide A
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isoform 2, pH and temperature not specified in the publication
1.8
6-tuliposide A
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isoform 1, pH and temperature not specified in the publication
3
6-tuliposide A
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isoform 3, pH and temperature not specified in the publication
7.4
6-tuliposide B
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isoform 3, pH and temperature not specified in the publication
8.7
6-tuliposide B
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isoform 2, pH and temperature not specified in the publication
9.5
6-tuliposide B
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isoform 1, pH and temperature not specified in the publication
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
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constitutive enzyme expression. The TCEs and 6-Pos are well separated by spatial compartmentation in intact tulip cells
brenda
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the enzyme is specifically expressed in the pollen grains, but not in the anther cells
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
the enzyme's transit peptide functions as a plastid-sorting signal for mature TCE polypeptides
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
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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
physiological function
physiological function
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
physiological function
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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
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). TCEB1_TULGE
440
0
49023
Swiss-Prot
Chloroplast (Reliability: 2)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
homodimer
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
proteolytic modification
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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
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
enzyme immobilization of TCEB for improved synthesis of PaB, overview
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
45 - 50
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the stable temperatures of the enzymes are up to 45°C for isoforms 1 and 2, and 50°C for isoform 3
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
butyl-Toyopearl column chromatography, DEAE-Toyopearl column chromatography, Resource Q column chromatography, and Superdex 75 gel filtration
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recombinant wild-type enzyme from Escherichia coli strain Rosetta 2 (DE3)/pET28a
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene TgTCEB1, recombinant expression of the wild-type enzyme in Escherichia coli strain Rosetta 2 (DE3)/pET28a
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
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
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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
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Nomura, T.; Murase, T.; Ogita, S.; Kato, Y.
Molecular identification of tuliposide B-converting enzyme: a lactone-forming carboxylesterase from the pollen of tulip
Plant J.
83
252-262
2015
Tulipa gesneriana
brenda
Nomura, T.; Ogita, S.; Kato, Y.
One-step enzymatic synthesis of 1-tuliposide a using tuliposide-converting enzyme
Appl. Biochem. Biotechnol.
188
12-28
2018
Tulipa gesneriana (I4DST8)
brenda
Nomura, T.
Function and application of a non-ester-hydrolyzing carboxylesterase discovered in tulip
Biosci. Biotechnol. Biochem.
81
81-94
2017
Tulipa gesneriana
brenda
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Release 2023.1 (January 2023)
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