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Information on EC 2.8.2.37 - trehalose 2-sulfotransferase

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EC Tree
     2 Transferases
         2.8 Transferring sulfur-containing groups
             2.8.2 Sulfotransferases
                2.8.2.37 trehalose 2-sulfotransferase
IUBMB Comments
The sulfation of trehalose in the bacterium Mycobacterium tuberculosis is required for the biosynthesis of sulfolipid-1.
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This record set is specific for:
UNIPROT: P84151
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The enzyme appears in viruses and cellular organisms
Synonyms
stf0 sulfotransferase, more
PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
3'-phosphoadenylyl-sulfate:alpha,alpha'-trehalose 2-sulfotransferase
The sulfation of trehalose in the bacterium Mycobacterium tuberculosis is required for the biosynthesis of sulfolipid-1.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
3'-phosphoadenylyl sulfate + alpha,alpha-trehalose
adenosine 3',5'-bisphosphate + 2-O-sulfo-alpha,alpha-trehalose
show the reaction diagram
3'-phosphoadenylyl sulfate + alpha-D-galactopyranosyl alpha-D-glucopyranoside
?
show the reaction diagram
alpha-D-galactopyranosyl-alpha-D-glucopyranoside is a synthetic analog of trehalose epimerized at a single stereocenter is sulfated 68fold less efficiently than trehalose
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?
additional information
?
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no activity on beta-phenyl glucoside, glucose, neo-trehalose or iso-trehalose
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-
?
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
3'-phosphoadenylyl sulfate + alpha,alpha-trehalose
adenosine 3',5'-bisphosphate + 2-O-sulfo-alpha,alpha-trehalose
show the reaction diagram
sulfotransferase Stf0 carries out the first committed step in the biosynthesis of sulfolipid SL-1
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-
?
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
6.4 - 29
alpha,alpha-trehalose
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.017 - 1.6
alpha,alpha-trehalose
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0026 - 0.89
alpha,alpha-trehalose
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
sulfotransferase Stf0 carries out the first committed step in the biosynthesis of sulfolipid SL-1
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
P84151_MYCSM
267
0
30291
TrEMBL
other Location (Reliability: 2)
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
vapor diffusion method, crystal structure of the enzyme bound to trehalose
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E33A
kcat/Km for trehalose is 4.2fold lower compared to wild-type value
E36A
kcat/Km for trehalose is 34.2fold lower compared to wild-type value
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Mougous, J.D.; Petzold, C.J.; Senaratne, R.H.; Lee, D.H.; Akey, D.L.; Lin, F.L.; Munchel, S.E.; Pratt, M.R.; Riley, L.W.; Leary, J.A.; Berger, J.M.; Bertozzi, C.R.
Identification, function and structure of the mycobacterial sulfotransferase that initiates sulfolipid-1 biosynthesis
Nat. Struct. Mol. Biol.
11
721-729
2004
Mycobacterium tuberculosis (O53699), Mycolicibacterium smegmatis (P84151)
Manually annotated by BRENDA team