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Information on EC 3.2.1.199 - sulfoquinovosidase and Organism(s) Escherichia coli and UniProt Accession P32138

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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 using a retaining mechanism. The enzyme belongs to the glycosyl hydrolase GH31 family.
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This record set is specific for:
Escherichia coli
UNIPROT: P32138
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The taxonomic range for the selected organisms is: Escherichia coli
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
sulfoquinovosidase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
PATHWAY SOURCE
PATHWAYS
-
-
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 using a retaining mechanism. The enzyme belongs to the glycosyl hydrolase GH31 family.
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
-
-
-
?
4-nitrophenyl alpha-sulfoquinovoside + H2O
6-sulfo-D-quinovose + 4-nitrophenol
show the reaction diagram
a sulfoquinovosyl diacylglyceride + H2O
6-sulfo-D-quinovose + a diacylglycerol
show the reaction diagram
-
complete conversion to sulfoquinose
-
?
2-hydroxyethyl sulfoquinovoside + H2O
?
show the reaction diagram
-
-
-
-
?
3-hydroxypropyl sulfoquinovoside + H2O
?
show the reaction diagram
-
-
-
-
?
a sulfoquinovosyl 2,3-diacylglyceride + H2O
6-sulfo-D-quinovose + a diacylglycerol
show the reaction diagram
-
-
complete conversion to sulfoquinose
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
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
-
complete conversion to sulfoquinose
-
?
INHIBITOR
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
-
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.15 - 4.28
4-nitrophenyl alpha-sulfoquinovoside
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.21 - 32.7
4-nitrophenyl alpha-sulfoquinovoside
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.1 - 218
4-nitrophenyl alpha-sulfoquinovoside
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7
-
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25
-
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
the enzyme enables sulfoglycolytic utilization of sulfoquinovosyl glycerol as sole carbon source
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SUBUNIT
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
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D405N
inactive
D472A
inactive
D472N
inactive
Q262K
1000fold decrease in activity
Q262K/Q288E
100fold decrease in activity
Q288E
mutation in active site, 1000fold decrease in activity
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
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
Manually annotated by BRENDA team
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 (P32138), Escherichia coli
Manually annotated by BRENDA team
Shibuya, I.; Benson, A.
Hydrolysis of alpha-sulphoquinovosides by beta-galactosidase
Nature
192
1186-1187
1961
Escherichia coli, Escherichia coli ML308
-
Manually annotated by BRENDA team
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 (P32138), Escherichia coli
Manually annotated by BRENDA team