Information on EC 3.2.1.199 - sulfoquinovosidase

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The expected taxonomic range for this enzyme is: Escherichia coli

EC NUMBER
COMMENTARY hide
3.2.1.199
-
RECOMMENDED NAME
GeneOntology No.
sulfoquinovosidase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
an 6-sulfo-alpha-D-quinovosyl diacylglycerol + H2O = 6-sulfo-D-quinovose + a 1,2-diacylglycerol
show the reaction diagram
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-
-
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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.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
1-sulfoquinovosylglycerol + H2O
6-sulfo-D-quinovose + glycerol
show the reaction diagram
-
-
-
?
2-hydroxyethyl sulfoquinovoside + H2O
?
show the reaction diagram
3-hydroxypropyl sulfoquinovoside + H2O
?
show the reaction diagram
4-nitrophenyl alpha-sulfoquinovoside + H2O
6-sulfo-D-quinovose + 4-nitrophenol
show the reaction diagram
-
-
-
?
a sulfoquinovosyl 2,3-diacylglyceride + H2O
6-sulfo-D-quinovose + a diacylglycerol
show the reaction diagram
a sulfoquinovosyl diacylglyceride + H2O
6-sulfo-D-quinovose + a diacylglycerol
show the reaction diagram
-
complete conversion to sulfoquinose
-
?
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
a sulfoquinovosyl diacylglyceride + H2O
6-sulfo-D-quinovose + a diacylglycerol
show the reaction diagram
P32138
-
complete conversion to sulfoquinose
-
?
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
5-fluoro-beta-L-idopyranosyl fluoride
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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-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.22
4-nitrophenyl alpha-sulfoquinovoside
pH not specified in the publication, temperature not specified in the publication
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
14.3
4-nitrophenyl alpha-sulfoquinovoside
Escherichia coli
P32138
pH not specified in the publication, temperature not specified in the publication
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
64
4-nitrophenyl alpha-sulfoquinovoside
Escherichia coli
P32138
pH not specified in the publication, temperature not specified in the publication
214075
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7
-
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25
-
assay at
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 77274, calculated, x * 70000, SDS-PAGE
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
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D405N
inactive
D472A
inactive
D472N
inactive