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Information on EC 4.2.99.22 - tuliposide A-converting enzyme
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EC Tree
4.2.99.22 tuliposide A-converting enzymeIUBMB Comments
Isolated from the plant Tulipa gesneriana (tulip). The reaction is an intramolecular transesterification producing the lactone. The enzyme also has a weak activity with 6-tuliposide B and 6-O-benzoyl-D-glucose.
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Word Map
- 4.2.99.22
-
tulipalins
- gesneriana
- carboxylesterase
- bulb
-
transesterification
- synthesis
- tfiis
The enzyme appears in viruses and cellular organisms
Synonyms
tcea1, tuliposide-converting enzyme, tuliposide a-converting enzyme, pos-converting enzyme, posa-converting enzyme, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
6-O-(4'-hydroxy-2'-methylenebutyryl)-D-glucose acyltransferase (lactone-forming)
-
-
-
-
PosA-converting enzyme
TCEA
tuliposide-converting enzyme
tuliposide-converting enzyme
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
6-tuliposide A = tulipalin A + D-glucose
-
-
-
-
6-tuliposide A = tulipalin A + 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 gamma-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 A D-glucose-lyase (tulipalin A forming)
Isolated from the plant Tulipa gesneriana (tulip). The reaction is an intramolecular transesterification producing the lactone. The enzyme also has a weak activity with 6-tuliposide B and 6-O-benzoyl-D-glucose.
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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
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 55% activity with PosF compared to 6-PosA, the configuration at the C-3' position of the substrate PosF is S-form
-
-
?
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 250% activity with PosD compared to 6-PosA, best substrate
-
-
?
6-tuliposide A
tulipalin A + D-glucose
-
enzyme accepts 6-tuliposide A to catalyze only the intramolecular transesterification but not the hydrolysis
-
?
6-tuliposide A
tulipalin A + D-glucose
i.e. 6-O-(4-hydroxy-2-methylenebutanoyl)-D-glucose
i.e. 2-methylenebutanolactone
-
?
6-tuliposide A
tulipalin A + D-glucose
i.e. 6-PosA, a monoacyl-glucose type of Pos, the enzyme catalyzes intramolecular transesterification, high activity
-
-
?
6-tuliposide B
tulipalin B + D-glucose
-
7.8% of the activity with 6-tuliposide A
-
-
?
6-tuliposide B
tulipalin B + D-glucose
8.7% of the activity with 6-tuliposide A
-
-
?
6-tuliposide B
tulipalin B + D-glucose
i.e. 6-PosB, a monoacyl-glucose type of Pos, the enzyme catalyzes intramolecular transesterification, the enzyme shows 4.6% activity with 6-PosB compared to 6-PosA
-
-
?
6-tuliposide B
tulipalin B + D-glucose
i.e. 6-PosB, enzyme TCEA shows 7-8% activity with 6-PosB compared to 6-PosA
-
-
?
additional information
?
-
TCE enzymes are lactone-forming enzymes and a non-ester-hydrolyzing carboxylesterase, and specifically catalyze intramolecular transesterification, but not hydrolysis
-
-
?
additional information
?
-
TCE enzymes are lactone-forming enzymes and a non-ester-hydrolyzing carboxylesterase, and specifically catalyze intramolecular transesterification, but not hydrolysis
-
-
?
additional information
?
-
6-tuliposide A (6-PosA) is chemically labile, and they can be spontaneously converted to PaA in neutral to weakly basic conditions in vitro. 1-Tuliposide A (1-PosA) is no substrate
-
-
?
additional information
?
-
enzyme TCEA preferentially catalyzes the conversion of 6-PosA to PaA, but it also shows activity for 6-PosB, at about 7-8% relative to that of 6-PosA. TCEA catalyzes intramolecular transesterification of 6-tuliposide A (6-PosA) to form tulipalins A (PaA), but neither the hydrolysis of 6-Pos nor Pa. 1alpha- and 1beta-anomers exist for 6-PosA, and both anomers serve as substrates for TCEA
-
-
?
additional information
?
-
enzyme TCEA preferentially catalyzes the conversion of 6-PosA to PaA, but it also shows activity for 6-PosB, at about 7-8% relative to that of 6-PosA. TCEA catalyzes intramolecular transesterification of 6-tuliposide A (6-PosA) to form tulipalins A (PaA), but neither the hydrolysis of 6-Pos nor Pa. 1alpha- and 1beta-anomers exist for 6-PosA, and both anomers serve as substrates for TCEA
-
-
?
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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
additional information
?
-
TCE enzymes are lactone-forming enzymes and a non-ester-hydrolyzing carboxylesterase, and specifically catalyze intramolecular transesterification, but not hydrolysis
-
-
?
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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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
phenylmethylsulfonyl fluoride
remarkably reduces the activity of the native enzyme purified from tulip; remarkably reduces the activity of the native enzyme purified from tulip
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Adenoma
CHCHD7-PLAG1 and TCEA1-PLAG1 gene fusions resulting from cryptic, intrachromosomal 8q rearrangements in pleomorphic salivary gland adenomas.
Neoplasms
TCEA3 binds to TGF-beta receptor I and induces Smad-independent, JNK-dependent apoptosis in ovarian cancer cells.
Pancreatic Neoplasms
TCEA3 binds to TGF-beta receptor I and induces Smad-independent, JNK-dependent apoptosis in ovarian cancer cells.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
Michaelis-Menten kinetics
-
12
6-tuliposide A
isoform TCEA-b1, pH not specified in the publication, temperature not specified in the publication
96
6-tuliposide B
isoform TCEA-b1, pH not specified in the publication, temperature not specified in the publication
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1400
6-tuliposide A
isoform TCEA-b1, pH not specified in the publication, temperature not specified in the publication
610
6-tuliposide B
isoform TCEA-b1, pH not specified in the publication, temperature not specified in the publication
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
120
6-tuliposide A
isoform TCEA-b1, pH not specified in the publication, temperature not specified in the publication
6.4
6-tuliposide B
isoform TCEA-b1, pH not specified in the publication, temperature not specified in the publication
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
1210
isoform TCEA-b1, pH not specified in the publication, temperature not specified in the publication
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.5
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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
additional information
gene TCEA1 is transcribed in all tissues except for bulbs
brenda
additional information
constitutive enzyme expression. The TCEs and 6-Pos are well separated by spatial compartmentation in intact tulip cells. The TCEA isozyme from bulbs results in the identification of the TgTCEA-b1 gene, which is similar to, but apparently different from, the TgTCEA1 gene from petals (approximately 77% identity at the amino acid level). The TgTCEA-b1 gene is transcribed preferentially in bulbs, in which TgTCEA1 transcripts are absent. It is likely that expression of each isozyme is transcriptionally regulated so as to allocate an isozyme that is most suitable to the physiological environment of each plastid type
brenda
additional information
constitutive enzyme expression. The TCEs and 6-Pos are well separated by spatial compartmentation in intact tulip cells. The TCEA isozyme from bulbs results in the identification of the TgTCEA-b1 gene, which is similar to, but apparently different from, the TgTCEA1 gene from petals (approximately 77% identity at the amino acid level). The TgTCEA-b1 gene is transcribed preferentially in bulbs, in which TgTCEA1 transcripts are absent. It is likely that expression of each isozyme is transcriptionally regulated so as to allocate an isozyme that is most suitable to the physiological environment of each plastid type
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
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
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
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). TCAB1_TULGE
374
0
40499
Swiss-Prot
Chloroplast (Reliability: 5)
TCAB2_TULGE
374
0
40499
Swiss-Prot
Chloroplast (Reliability: 5)
TCAB3_TULGE
374
0
40456
Swiss-Prot
Chloroplast (Reliability: 4)
TCAB4_TULGE
374
0
40482
Swiss-Prot
Chloroplast (Reliability: 5)
TCEA1_TULGE
385
0
41511
Swiss-Prot
Chloroplast (Reliability: 3)
TCEA2_TULGE
382
0
41140
Swiss-Prot
Chloroplast (Reliability: 3)
A0A5B6YTX7_DAVIN
105
0
12032
TrEMBL
other Location (Reliability: 2)
A0A5B7C1G4_DAVIN
121
0
13322
TrEMBL
other Location (Reliability: 1)
A0A5B7BMS9_DAVIN
355
0
39758
TrEMBL
other Location (Reliability: 4)
A0A5B7C3C8_DAVIN
321
0
35772
TrEMBL
Secretory Pathway (Reliability: 5)
A0A5B7C326_DAVIN
163
0
17869
TrEMBL
other Location (Reliability: 2)
A0A5B6ZG75_DAVIN
141
0
15347
TrEMBL
other Location (Reliability: 3)
A0A5B6ZCJ3_DAVIN
348
0
38728
TrEMBL
other Location (Reliability: 3)
A0A5B7CC99_DAVIN
109
0
12307
TrEMBL
other Location (Reliability: 4)
A0A5B7BXI6_DAVIN
306
0
33643
TrEMBL
other Location (Reliability: 3)
A0A5B6YRT7_DAVIN
325
0
35735
TrEMBL
other Location (Reliability: 3)
A0A5B6YRG6_DAVIN
653
0
71852
TrEMBL
Secretory Pathway (Reliability: 2)
A0A5B7B9N5_DAVIN
313
0
34612
TrEMBL
other Location (Reliability: 2)
A0A5B6ZIX3_DAVIN
361
0
40120
TrEMBL
Chloroplast (Reliability: 5)
A0A2G9HSE3_9LAMI
303
0
33964
TrEMBL
other Location (Reliability: 3)
A0A5B7C2X6_DAVIN
302
0
33379
TrEMBL
other Location (Reliability: 2)
A0A5B7C3N8_DAVIN
340
0
37519
TrEMBL
other Location (Reliability: 3)
A0A5B6ZDB3_DAVIN
366
0
40474
TrEMBL
Secretory Pathway (Reliability: 3)
A0A5B6YSZ3_DAVIN
105
0
12032
TrEMBL
other Location (Reliability: 2)
A0A5B7CCB3_DAVIN
316
0
35142
TrEMBL
other Location (Reliability: 3)
A0A5B7CAV9_DAVIN
334
0
36830
TrEMBL
other Location (Reliability: 5)
A0A5B7BD81_DAVIN
302
0
33246
TrEMBL
other Location (Reliability: 2)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
34000
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
homodimer
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
proteolytic modification
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
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant wild-type enzyme from Escherichia coli BL21-CodonPlus (DE3)-RIL/pET28a
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene TgTCEA1, recombinant expression of the wild-type enzyme in Escherichia coli BL21-CodonPlus (DE3)-RIL/pET28a
gene TgTCEA1, 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 TCEA in onion epidermal cell plastids
TCEA-b genes b1-b7 are higly homologous to each other, with six to seven single-nucleotide polymorphisms
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
synthesis
-
facile method of enzyme-mediated conversion of 6-tuliposide to alpha-methylene-gamma-butyrolactone, i.e.tulipalin by use of a tuliposide-converting enzyme for the conversion of 6-tuliposides. 6-Tuliposides are extracted from tulip tissues into the corresponding tulipalins in high yields within 2 h at pH 7.0. The resulting tulipalins are selectively extracted by using several organic solvents
synthesis
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
Kato, Y.; Shoji, K.; Ubukata, M.; Shigetomi, K.; Sato, Y.; Nakajima, N.; Ogita, S.
Purification and characterization of a tuliposide-converting enzyme from bulbs of Tulipa gesneriana
Biosci. Biotechnol. Biochem.
73
1895-1897
2009
Tulipa gesneriana
brenda
Nomura, T.; Tsuchigami, A.; Ogita, S.; Kato, Y.
Molecular diversity of tuliposide A-converting enzyme in the tulip
Biosci. Biotechnol. Biochem.
77
1042-1048
2013
Tulipa gesneriana (R4X244)
brenda
Nomura, T.; Ogita, S.; Kato, Y.
A novel lactone-forming carboxylesterase: molecular identification of a tuliposide A-converting enzyme in tulip
Plant Physiol.
159
565-578
2012
Tulipa gesneriana (I4DST8)
brenda
Kato, Y.; Yoshida, H.; Shoji, K.; Sato, Y.; Nakajima, N.; Ogita, S.
A facile method for the preparation of alpha-methylene-gamma-butyrolactones from tulip tissues by enzyme-mediated conversion
Tetrahedron Lett.
50
4751-4753
2009
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 (I4DST8), Tulipa gesneriana (R4X244)
brenda
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