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Information on EC 3.1.1.49 - sinapine esterase
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3.1.1.49 sinapine esteraseSpecify your search results
Word Map
- 3.1.1.49
- napus
- seedlings
-
brassica
- brassicaceae
- sinapate
-
antinutritive
- sinapoylmalate
- lipases
The enzyme appears in viruses and cellular organisms
Synonyms
bnlip2, sinapine esterase, bnsce3, bnsce3/bnlip2, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
BnSCE3
SCE
sinapoylcholine(sinapine) esterase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
sinapoylcholine + H2O = sinapate + choline
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SYSTEMATIC NAME
IUBMB Comments
sinapoylcholine sinapohydrolase
-
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CAS REGISTRY NUMBER
COMMENTARY
72506-67-3
-
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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
4-coumaroylcholine + H2O
coumaric acid + choline
20% of activity with sinapoylcholine
-
?
benzoylcholine + H2O
benzoate + choline
18% of activity with sinapoylcholine
-
?
additional information
?
-
-
BnSCE3 reveals a broad substrate specificity toward phenolic choline esters, even accepting phosphatidylcholine, pointing to a phospholipase A-like activity
-
?
caffeoylcholine
caffeic acid + choline
25% of activity with sinapoylcholine
-
?
cinnamoylcholine + H2O
cinnamic acid + choline
51% of activity with sinapoylcholine
-
?
feruloylcholine + H2O
ferulic acid + choline
37% of activity with sinapoylcholine
-
?
O-sinapoylcholine + H2O
choline + sinapate
i.e. sinapine
-
?
sinapoylcholine + H2O
sinapic acid + choline
role for the GDSL lipase-like BnSCE3/BnLIP2 as a sinapine esterase, catalyzing hydrolysis of sinapine during seed germination, leading, via 1-O-sinapoyl-beta-glucose, to sinapoyl-L-malate in the seedlings
-
?
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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
sinapoylcholine + H2O
sinapic acid + choline
role for the GDSL lipase-like BnSCE3/BnLIP2 as a sinapine esterase, catalyzing hydrolysis of sinapine during seed germination, leading, via 1-O-sinapoyl-beta-glucose, to sinapoyl-L-malate in the seedlings
-
-
?
additional information
?
-
-
BnSCE3 reveals a broad substrate specificity toward phenolic choline esters, even accepting phosphatidylcholine, pointing to a phospholipase A-like activity
-
-
?
O-sinapoylcholine + H2O
choline + sinapate
i.e. sinapine
-
-
?
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
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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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE RANGE
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
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
metabolism
physiological function
additional information
evolution
-
BnSCE3 is classifed as a member of the SGNH hydrolase subfamily of GDSL-lipases which cleave ester bonds in a wide array of lipids. Sinapine esterase BnSCE3 kept the catalytic mechanism of the hydrolytic ancestor but experienced a change in substrate specificity
evolution
sinapine esterase is classifed as a member of the SGNH hydrolase subfamily of GDSL-lipases which cleave ester bonds in a wide array of lipids
metabolism
-
1-O-sinapoylglucose, produced by UDP-glucose:sinapate glucosyltransferase during seed development, is converted to sinapine by sinapoylglucose:choline sinapoyltransferase and hydrolyzed by sinapoylcholine (sinapine) esterase in germinating seeds. The released sinapate feeds via sinapoylglucose into the biosynthesis of sinapoylmalate in the seedlings catalyzed by sinapoylglucose:L-malate sinapoyltransferase. Pathway of sinapate ester biosynthesis, overview
metabolism
1-O-sinapoylglucose, produced by UDP-glucose:sinapate glucosyltransferase during seed development, is converted to sinapine by sinapoylglucose:choline sinapoyltransferase and hydrolyzed by sinapoylcholine (sinapine) esterase in germinating seeds. The released sinapate feeds via sinapoylglucose into the biosynthesis of sinapoylmalate in the seedlings catalyzed by sinapoylglucose:L-malate sinapoyltransferase. Pathway of sinapate ester biosynthesis, overview
metabolism
-
a portion of choline enters the phospholipid metabolism, and sinapate is routed via 1-O-sinapoyl-beta-D-glucose into sinapoylmalate
physiological function
-
during early stages of seedling development, a sinapine esterase BnSCE3 hydrolyzes sinapine, releasing choline and sinapate, metabolic changes in developing seedlings of wild-type and enzyme overexpressing plants, overview
physiological function
sinapoylmalate is involved in protecting the leaves against the deleterious effects of UV-B radiation. Sinapine might function as storage vehicle for ready supply of choline for phosphatidylcholine biosynthesis in young seedlings
physiological function
-
sinapoylmalate is involved in protecting the leaves against the deleterious effects of UV-B radiation. Sinapine might function as storage vehicle for ready supply of choline for phosphatidylcholine biosynthesis in young seedlings. Antinutritive character of sinapine and related sinapate esters
additional information
-
profiling of secondary metabolites and comparison in wild-type and transgenic seeds, overview
additional information
-
SCE activity in seedlings of Brassica napus is mediated by a GDSL lipase-like enzyme designated as BnSCE3, one of three detected SCE isoforms
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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). SCE3_BRANA
389
0
43319
Swiss-Prot
Secretory Pathway (Reliability: 1)
G8A2E1_MEDTR
361
1
40019
TrEMBL
Secretory Pathway (Reliability: 1)
A0A2G9HMU5_9LAMI
406
0
44676
TrEMBL
other Location (Reliability: 5)
A0A2G9I0J8_9LAMI
394
1
43124
TrEMBL
Secretory Pathway (Reliability: 1)
A0A396JEK6_MEDTR
359
0
39944
TrEMBL
Secretory Pathway (Reliability: 1)
A0A396IXJ1_MEDTR
307
0
34548
TrEMBL
other Location (Reliability: 4)
A0A396JTN2_MEDTR
219
0
24785
TrEMBL
other Location (Reliability: 3)
A0A072VKA1_MEDTR
348
1
38733
TrEMBL
Secretory Pathway (Reliability: 1)
A0A2G9I0P7_9LAMI
394
1
43488
TrEMBL
Secretory Pathway (Reliability: 1)
A0A396JEX3_MEDTR
317
0
35261
TrEMBL
Secretory Pathway (Reliability: 2)
A0A2P6Q4L2_ROSCH
363
0
39578
TrEMBL
Secretory Pathway (Reliability: 1)
A0A072TJ60_MEDTR
359
0
39951
TrEMBL
Secretory Pathway (Reliability: 1)
A0A2G9HMS2_9LAMI
94
1
10123
TrEMBL
Secretory Pathway (Reliability: 1)
A0A2G9HNH0_9LAMI
94
0
10597
TrEMBL
other Location (Reliability: 3)
A0A2G9I0L9_9LAMI
282
1
30607
TrEMBL
other Location (Reliability: 5)
A0A396J5Y8_MEDTR
300
0
33284
TrEMBL
Secretory Pathway (Reliability: 1)
A0A2G9I0L8_9LAMI
400
0
44111
TrEMBL
Chloroplast (Reliability: 4)
A0A396J6B9_MEDTR
317
0
35379
TrEMBL
Secretory Pathway (Reliability: 2)
A0A072TK31_MEDTR
359
0
40005
TrEMBL
Secretory Pathway (Reliability: 1)
A0A2G9HMT8_9LAMI
481
0
53015
TrEMBL
Mitochondrion (Reliability: 3)
A0A396IPH8_MEDTR
388
1
43509
TrEMBL
Secretory Pathway (Reliability: 1)
G7IKA5_MEDTR
399
0
44141
TrEMBL
Mitochondrion (Reliability: 5)
A0A2P6P5A1_ROSCH
383
0
42042
TrEMBL
Secretory Pathway (Reliability: 4)
A0A2G9HMV2_9LAMI
237
0
26433
TrEMBL
other Location (Reliability: 3)
A0A396JA90_MEDTR
359
0
39919
TrEMBL
Secretory Pathway (Reliability: 1)
G7IKA9_MEDTR
387
1
43142
TrEMBL
Secretory Pathway (Reliability: 1)
A0A2P6Q4L4_ROSCH
370
1
40919
TrEMBL
Secretory Pathway (Reliability: 1)
A0A2G9I0K0_9LAMI
402
0
44079
TrEMBL
other Location (Reliability: 5)
A0A2G9I753_9LAMI
389
0
42746
TrEMBL
Secretory Pathway (Reliability: 1)
A0A396J6B3_MEDTR
361
1
40147
TrEMBL
Secretory Pathway (Reliability: 1)
G7IKA6_MEDTR
375
1
41715
TrEMBL
Secretory Pathway (Reliability: 1)
G7IKB1_MEDTR
374
0
41071
TrEMBL
Secretory Pathway (Reliability: 3)
A0A2G9I3G4_9LAMI
363
0
39815
TrEMBL
other Location (Reliability: 3)
A0A396JAU8_MEDTR
285
1
31718
TrEMBL
Secretory Pathway (Reliability: 1)
A0A2G9HN27_9LAMI
388
0
42806
TrEMBL
Secretory Pathway (Reliability: 2)
A0A2G9HMT1_9LAMI
203
0
22957
TrEMBL
other Location (Reliability: 3)
A0A2G9I0M9_9LAMI
389
0
42749
TrEMBL
Secretory Pathway (Reliability: 1)
A0A2G9I114_9LAMI
200
0
22221
TrEMBL
other Location (Reliability: 2)
A0A396J224_MEDTR
67
1
8032
TrEMBL
other Location (Reliability: 2)
A0A396JBC7_MEDTR
255
0
28584
TrEMBL
Secretory Pathway (Reliability: 2)
A0A2G9HMU4_9LAMI
364
0
40138
TrEMBL
Secretory Pathway (Reliability: 2)
A0A2G9I0J6_9LAMI
388
0
42646
TrEMBL
Secretory Pathway (Reliability: 2)
A0A2G9I3G8_9LAMI
383
0
41789
TrEMBL
Secretory Pathway (Reliability: 2)
A0A2G9HMV8_9LAMI
208
0
22832
TrEMBL
Chloroplast (Reliability: 4)
A0A396I708_MEDTR
210
0
23753
TrEMBL
other Location (Reliability: 5)
G7JA29_MEDTR
369
0
41254
TrEMBL
Secretory Pathway (Reliability: 1)
G7JMN9_MEDTR
380
0
42429
TrEMBL
Secretory Pathway (Reliability: 2)
A0A2P6SBX3_ROSCH
243
0
26938
TrEMBL
other Location (Reliability: 3)
A0A2P6Q4I5_ROSCH
181
0
20303
TrEMBL
Secretory Pathway (Reliability: 1)
A0A2G9HMU3_9LAMI
365
0
40051
TrEMBL
Secretory Pathway (Reliability: 3)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
sinapine levels of transgenic seeds are less than 5% of wild-type levels, whereas choline levels are increased. Weight, size, and water content of transgenic seeds are significantly higher than those of wild-type seeds, phenotype, overveiw
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
functional expression of Brassica napus BnSCE3 in Arabidopsis thaliana developing seeds resulting in a dramatic decrease in the sinapine content
-
gene At1g28640, the BnSCE3 homologue is tagged on chromosome I
gene At1g28650, the BnSCE3 homologue is tagged on chromosome I
gene At1g28660, the BnSCE3 homologue is tagged on chromosome I
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Nurmann, G.; Strack, D.
Sinapine esterase. 1. Characterization of sinapine esterase from cotyledons of Raphanus sativus
Z. Naturforsch. C
34
715-720
1979
Raphanus sativus
-
brenda
Strack, D.; Nurmann, G.; Sachs, G.
Sinapine esterase. II. Specificity and change of sinapine esterase activity during germination of Raphanus sativus
Z. Naturforsch. C
35
963-966
1980
Brassica oleracea, Camelina sativa, Raphanus sativus, Sinapis alba
-
brenda
Larsen, L.M.; Nielsen, T.H.; Plöger, A.; Sorensen, H.
Rapid and efficient method for the isolation and characterization of plant aromatic choline esterases
J. Chromatogr.
450
121-131
1988
Barbarea intermedia, Brassica rapa subsp. oleifera, Brassica napus, Brassica nigra, Sinapis alba
-
brenda
Clauss, K.; Baumert, A.; Nimtz, M.; Milkowski, C.; Strack, D.
Role of a GDSL lipase-like protein as sinapine esterase in Brassicaceae
Plant J.
53
802-813
2008
Brassica napus (Q3ZFI4), Brassica napus
brenda
Clauss, K.; von Roepenack-Lahaye, E.; Boettcher, C.; Roth, M.R.; Welti, R.; Erban, A.; Kopka, J.; Scheel, D.; Milkowski, C.; Strack, D.
Overexpression of sinapine esterase BnSCE3 in oilseed rape seeds triggers global changes in seed metabolism
Plant Physiol.
155
1127-1145
2011
Brassica napus
brenda
Milkowski, C.; Strack, D.
Sinapate esters in brassicaceous plants: biochemistry, molecular biology, evolution and metabolic engineering
Planta
232
19-35
2010
Brassica napus, Arabidopsis thaliana (P0C8Z7), Arabidopsis thaliana (Q38894), Arabidopsis thaliana (Q3E7I6), Arabidopsis thaliana (Q9FPE4)
brenda
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