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Enzyme Nomenclature
Information on EC 3.2.1.199 - sulfoquinovosidase
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3.2.1.199 sulfoquinovosidaseIUBMB 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.
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The enzyme appears in viruses and cellular organisms
Reaction Schemes
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
yihQ
yihQ
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
an 6-sulfo-alpha-D-quinovosyl diacylglycerol + H2O = 6-sulfo-D-quinovose + a 1,2-diacylglycerol
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-
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-
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PATHWAY SOURCE
PATHWAYS
MetaCyc
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SYSTEMATIC NAME
IUBMB Comments
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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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-sulfoquinovosylglycerol + H2O
6-sulfo-D-quinovose + glycerol
-
-
-
?
a sulfoquinovosyl diacylglyceride + H2O
6-sulfo-D-quinovose + a diacylglycerol
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complete conversion to sulfoquinose
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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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-
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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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-
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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
a sulfoquinovosyl diacylglyceride + H2O
6-sulfo-D-quinovose + a diacylglycerol
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complete conversion to sulfoquinose
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?
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.15
4-nitrophenyl alpha-sulfoquinovoside
-
wild-type, pH not specified in the publication, temperature not specified in the publication
0.212
4-nitrophenyl alpha-sulfoquinovoside
-
wild-type, pH not specified in the publication, temperature not specified in the publication
0.22
4-nitrophenyl alpha-sulfoquinovoside
-
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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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
-
wild-type, 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
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
-
mutant E270Q, pH not specified in the publication, temperature not specified in the publication
0.1
4-nitrophenyl alpha-sulfoquinovoside
-
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
-
mutantK245Q/ E270Q, pH not specified in the publication, temperature not specified in the publication
64
4-nitrophenyl alpha-sulfoquinovoside
-
pH not specified in the publication, temperature not specified in the publication
105
4-nitrophenyl alpha-sulfoquinovoside
-
wild-type, pH not specified in the publication, temperature not specified in the publication
218
4-nitrophenyl alpha-sulfoquinovoside
-
wild-type, pH not specified in the publication, temperature not specified in the publication
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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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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
physiological function
-
the enzyme enables sulfoglycolytic utilization of sulfoquinovosyl glycerol as sole carbon source
physiological function
-
the enzyme enables sulfoglycolytic utilization of sulfoquinovosyl glycerol as sole carbon source
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
Sequence
A0A4V1CUC8_SHIFM
Shigella flexneri serotype 5a (strain M90T)
678
0
77305
TrEMBL
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PDB
SCOP
CATH
UNIPROT
ORGANISM
Escherichia coli (strain K12)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
-
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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