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Information on EC 3.2.1.199 - sulfoquinovosidase for references in articles please use BRENDA:EC3.2.1.199
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EC Tree
IUBMB Comments The enzyme, characterized from the bacteria Escherichia coli and Pseudomonas putida, hydrolyses terminal non-reducing alpha-sulfoquinovoside residues in alpha-sulfoquinovosyl diacylglycerides and alpha-sulfoquinovosyl glycerol.
The enzyme appears in viruses and cellular organisms
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yihQ
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an 6-sulfo-alpha-D-quinovosyl diacylglycerol + H2O = 6-sulfo-D-quinovose + a 1,2-diacylglycerol
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6-sulfo-alpha-D-quinovosyl diacylglycerol 6-sulfo-D-quinovohydrolase
The enzyme, characterized from the bacteria Escherichia coli and Pseudomonas putida, hydrolyses terminal non-reducing alpha-sulfoquinovoside residues in alpha-sulfoquinovosyl diacylglycerides and alpha-sulfoquinovosyl glycerol.
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1-sulfoquinovosylglycerol + H2O
6-sulfo-D-quinovose + glycerol
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2-hydroxyethyl sulfoquinovoside + H2O
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3-hydroxypropyl sulfoquinovoside + H2O
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4-nitrophenyl alpha-sulfoquinovoside + H2O
6-sulfo-D-quinovose + 4-nitrophenol
a sulfoquinovosyl 2,3-diacylglyceride + H2O
6-sulfo-D-quinovose + a diacylglycerol
a sulfoquinovosyl diacylglyceride + H2O
6-sulfo-D-quinovose + a diacylglycerol
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complete conversion to sulfoquinose
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additional information
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2-hydroxyethyl sulfoquinovoside + H2O
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2-hydroxyethyl sulfoquinovoside + H2O
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3-hydroxypropyl sulfoquinovoside + H2O
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3-hydroxypropyl sulfoquinovoside + H2O
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4-nitrophenyl alpha-sulfoquinovoside + H2O
6-sulfo-D-quinovose + 4-nitrophenol
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4-nitrophenyl alpha-sulfoquinovoside + H2O
6-sulfo-D-quinovose + 4-nitrophenol
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4-nitrophenyl alpha-sulfoquinovoside + H2O
6-sulfo-D-quinovose + 4-nitrophenol
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a sulfoquinovosyl 2,3-diacylglyceride + H2O
6-sulfo-D-quinovose + a diacylglycerol
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complete conversion to sulfoquinose
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a sulfoquinovosyl 2,3-diacylglyceride + H2O
6-sulfo-D-quinovose + a diacylglycerol
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complete conversion to sulfoquinose
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additional information
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no substrates: 4-nitrophenyl alpha-D-sulfofucoside, 4-nitrophenyl alpha-D-sulforhamnoside, 4-nitrophenyl alpha-D-glucuronoside, 4-nitrophenyl alpha-D-glucopyranoside
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additional information
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enzyme shows weak activities on isomaltose, D-glucosyl fluoride and 4-nitrophenyl alpha-glucoside, but the hydrolytic activities on maltose, kojibiose, nigerose, trehalose, isomaltotriose, glucose 1-phosphate, panose, alpha-maltosyl fluoride, alpha-xylosyl Xuoride, 4-nitrophenyl alpha-xyloside, and isoprimeverose are under detectable limits
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additional information
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no substrate: 4-nitrophenyl alpha-D-glucopyranoside
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additional information
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no substrate: 4-nitrophenyl alpha-D-glucopyranoside
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additional information
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no substrates: methyl sulfoquinovoside, ethyl sulfoquinovoside, n-propyl sulfoquinovoside
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additional information
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no substrates: 4-nitrophenyl alpha-D-sulfofucoside, 4-nitrophenyl alpha-D-sulforhamnoside, 4-nitrophenyl alpha-D-glucuronoside
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additional information
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no substrates: methyl sulfoquinovoside, ethyl sulfoquinovoside, n-propyl sulfoquinovoside
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a sulfoquinovosyl diacylglyceride + H2O
6-sulfo-D-quinovose + a diacylglycerol
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complete conversion to sulfoquinose
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5-fluoro-beta-L-idopyranosyl fluoride
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mechanism-based inactivator, soaking of crystals yields a covalent glycosyl-enzyme complex in a 1S3 pyranose conformation
beta-D-galactopyranosyl glycerol
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0.15 - 4.45
4-nitrophenyl alpha-sulfoquinovoside
0.15
4-nitrophenyl alpha-sulfoquinovoside
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wild-type, pH not specified in the publication, temperature not specified in the publication
0.212
4-nitrophenyl alpha-sulfoquinovoside
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wild-type, pH not specified in the publication, temperature not specified in the publication
0.22
4-nitrophenyl alpha-sulfoquinovoside
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pH not specified in the publication, temperature not specified in the publication
1.29
4-nitrophenyl alpha-sulfoquinovoside
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mutant E270Q, pH not specified in the publication, temperature not specified in the publication
1.64
4-nitrophenyl alpha-sulfoquinovoside
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mutant K245Q, pH not specified in the publication, temperature not specified in the publication
2.07
4-nitrophenyl alpha-sulfoquinovoside
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mutant Q262K, pH not specified in the publication, temperature not specified in the publication
4.28
4-nitrophenyl alpha-sulfoquinovoside
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mutant Q262K/Q288E, pH not specified in the publication, temperature not specified in the publication
4.45
4-nitrophenyl alpha-sulfoquinovoside
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mutantK245Q/ E270Q, pH not specified in the publication, temperature not specified in the publication
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0.023 - 32.7
4-nitrophenyl alpha-sulfoquinovoside
0.023
4-nitrophenyl alpha-sulfoquinovoside
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mutant E270Q, pH not specified in the publication, temperature not specified in the publication
0.026
4-nitrophenyl alpha-sulfoquinovoside
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mutant K245Q, pH not specified in the publication, temperature not specified in the publication
0.21
4-nitrophenyl alpha-sulfoquinovoside
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mutant Q262K, pH not specified in the publication, temperature not specified in the publication
1.89
4-nitrophenyl alpha-sulfoquinovoside
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mutantK245Q/ E270Q, pH not specified in the publication, temperature not specified in the publication
11.2
4-nitrophenyl alpha-sulfoquinovoside
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mutant Q262K/Q288E, pH not specified in the publication, temperature not specified in the publication
14.3
4-nitrophenyl alpha-sulfoquinovoside
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pH not specified in the publication, temperature not specified in the publication
22.3
4-nitrophenyl alpha-sulfoquinovoside
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wild-type, pH not specified in the publication, temperature not specified in the publication
32.7
4-nitrophenyl alpha-sulfoquinovoside
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wild-type, pH not specified in the publication, temperature not specified in the publication
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0.016 - 218
4-nitrophenyl alpha-sulfoquinovoside
0.016
4-nitrophenyl alpha-sulfoquinovoside
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mutant K245Q, pH not specified in the publication, temperature not specified in the publication
0.018
4-nitrophenyl alpha-sulfoquinovoside
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mutant E270Q, pH not specified in the publication, temperature not specified in the publication
0.1
4-nitrophenyl alpha-sulfoquinovoside
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mutant Q262K, pH not specified in the publication, temperature not specified in the publication
0.48
4-nitrophenyl alpha-sulfoquinovoside
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mutant Q288E, pH not specified in the publication, temperature not specified in the publication
2.61
4-nitrophenyl alpha-sulfoquinovoside
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mutant Q262K/Q288E, pH not specified in the publication, temperature not specified in the publication
40.43
4-nitrophenyl alpha-sulfoquinovoside
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mutantK245Q/ E270Q, pH not specified in the publication, temperature not specified in the publication
64
4-nitrophenyl alpha-sulfoquinovoside
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pH not specified in the publication, temperature not specified in the publication
105
4-nitrophenyl alpha-sulfoquinovoside
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wild-type, pH not specified in the publication, temperature not specified in the publication
218
4-nitrophenyl alpha-sulfoquinovoside
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wild-type, pH not specified in the publication, temperature not specified in the publication
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brenda
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UniProt
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physiological function
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the enzyme enables sulfoglycolytic utilization of sulfoquinovosyl glycerol as sole carbon source
physiological function
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the enzyme enables sulfoglycolytic utilization of sulfoquinovosyl glycerol as sole carbon source
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SQASE_ECOLI
Escherichia coli (strain K12)
678
0
77275
Swiss-Prot
A0A0A1AF71_ECOLX
678
0
77207
TrEMBL
A0A4C9XBR2_ECOLX
678
0
77335
TrEMBL
A0A271U4T0_ECOLX
678
0
77350
TrEMBL
A0A0K5J1L7_ECOLX
678
0
77302
TrEMBL
A0A5N8HL72_ECOLX
300
0
33822
TrEMBL
A0A4T2KZP9_ECOLX
678
0
77188
TrEMBL
A0A4Y8GHT7_ECOLX
678
0
77278
TrEMBL
A0A5Q3GWV5_ECOLX
667
0
75890
TrEMBL
A0A4S5AVD1_ECOLI
Escherichia coli (strain K12)
678
0
77285
TrEMBL
A0A5B9AN36_ECOLX
678
0
77127
TrEMBL
A0A0L6Y1H3_ECOLX
678
0
77360
TrEMBL
A0A0B0VTI9_ECOLX
678
0
77211
TrEMBL
A0A5E7XZN3_9SPHN
669
0
74189
TrEMBL
A0A1V3W1C7_ECOLX
667
0
75860
TrEMBL
A0A2H5XT34_9BACT
682
0
78314
TrEMBL
A0A2T1M7Q1_ECOLX
678
0
77285
TrEMBL
A0A037YI49_ECOLX
678
0
77275
TrEMBL
A0A0F3V5W2_ECOLX
678
0
77261
TrEMBL
A0A5C0FPG3_ECOLX
678
0
77302
TrEMBL
A0A0F3T268_ECOLX
678
0
77289
TrEMBL
A0A0C2ED95_ECOLX
678
0
77261
TrEMBL
C3SJK2_ECOLX
678
0
77377
TrEMBL
A0A1M2IMJ9_ECOLX
678
0
77144
TrEMBL
A0A0A6UTS4_ECOLX
678
0
77265
TrEMBL
A0A0H0S2B8_ECOLX
678
0
77275
TrEMBL
A0A1Y2XLJ7_ECOLX
678
0
77378
TrEMBL
A0A2Y2KWK9_SHIFL
678
0
77305
TrEMBL
A0A557R4Z8_ECOLX
678
0
77261
TrEMBL
A0A148HI95_ECOLX
678
0
77196
TrEMBL
A0A5Q3STX1_ECOLX
678
0
77259
TrEMBL
Q8X8E8_ECO57
678
0
77377
TrEMBL
A0A024L6L3_ECOLX
678
0
77348
TrEMBL
A0A0D0N7T4_ECOLX
678
0
77247
TrEMBL
A0A5C2EIN6_SHIFL
678
0
77305
TrEMBL
A0A5P0Z4F1_ECOLX
678
0
77259
TrEMBL
A0A5E9S3P9_ECOLX
678
0
77301
TrEMBL
A0A5C0JEP3_ECOLX
678
0
77275
TrEMBL
A0A1Z3UWY9_ECOLX
678
0
77377
TrEMBL
A0A0V9NVW8_ECOLX
678
0
77349
TrEMBL
A0A5Q3TEY8_9ENTR
678
0
77275
TrEMBL
A0A5E4RDG2_9BURK
633
0
70878
TrEMBL
A0A4V1CUC8_SHIFM
Shigella flexneri serotype 5a (strain M90T)
678
0
77305
TrEMBL
A0A4S5A732_ECOLI
Escherichia coli (strain K12)
678
0
77285
TrEMBL
A0A1X0YL04_ECOLX
678
0
77341
TrEMBL
A0A0D8WJ76_ECOLX
678
0
77280
TrEMBL
A0A5B1EH94_ECOLX
678
0
77378
TrEMBL
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Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
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x * 77274, calculated, x * 70000, SDS-PAGE
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structure reveals an (alphabeta)8 barrel appended with a small beta-sheet domain. Residue D405 fulfills the role of catalytic nucleophile and D472 acts as a general acid-base
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E270Q
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1000fold decrease in activity
K245Q
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1000fold decrease in activity
K245Q/E270Q
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100fold decrease in activity
Q262K
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1000fold decrease in activity
Q262K/Q288E
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100fold decrease in activity
Q288E
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mutation in active site, 1000fold decrease in activity
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expression in Escherichia coli
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Okuyama, M.; Mori, H.; Chiba, S.; Kimura A.
Overexpression and characterization of two unknown proteins, YicI and YihQ, originated from Escherichia coli
Protein Expr. Purif.
37
170-179
2004
Escherichia coli
brenda
Speciale, G.; Jin, Y.; Davies, G.J.; Williams, S.J.; Goddard-Borger, E.D.
YihQ is a sulfoquinovosidase that cleaves sulfoquinovosyl diacylglyceride sulfolipids
Nat. Chem. Biol.
12
215-217
2016
Escherichia coli, Escherichia coli (P32138)
brenda
Shibuya, I.; Benson, A.
Hydrolysis of alpha-sulphoquinovosides by beta-galactosidase
Nature
192
1186-1187
1961
Escherichia coli, Escherichia coli ML308
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brenda
Abayakoon, P.; Jin, Y.; Lingford, J.P.; Petricevic, M.; John, A.; Ryan, E.; Wai-Ying Mui, J.; Pires, D.E.V.; Ascher, D.B.; Davies, G.J.; Goddard-Borger, E.D.; Williams, S.J.
Structural and biochemical insights into the function and evolution of sulfoquinovosidases
ACS Cent. Sci.
4
1266-1273
2018
Agrobacterium tumefaciens, Escherichia coli, Escherichia coli (P32138)
brenda
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