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Information on EC 2.3.1.288 - 2-O-sulfo trehalose long-chain-acyltransferase and Organism(s) Mycobacterium tuberculosis and UniProt Accession P9WIK7

for references in articles please use BRENDA:EC2.3.1.288
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IUBMB Comments
This mycobacterial enzyme catalyses the acylation of 2-O-sulfo-alpha,alpha-trehalose at the 2' position by a C16 or C18 fatty acyl group during the biosynthesis of mycobacterial sulfolipids.
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This record set is specific for:
Mycobacterium tuberculosis
UNIPROT: P9WIK7
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The taxonomic range for the selected organisms is: Mycobacterium tuberculosis
The expected taxonomic range for this enzyme is: Mycobacterium tuberculosis
Synonyms
rv3820c, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
trehalose-2-sulfate acyltransferase
-
papA2
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-
SYSTEMATIC NAME
IUBMB Comments
acyl-CoA:2-O-sulfo-alpha,alpha-trehalose 2'-long-chain-acyltransferase
This mycobacterial enzyme catalyses the acylation of 2-O-sulfo-alpha,alpha-trehalose at the 2' position by a C16 or C18 fatty acyl group during the biosynthesis of mycobacterial sulfolipids.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
palmitoyl-CoA + 2-O-sulfo-alpha,alpha-trehalose
2-O-sulfo-2'-palmitoyl-alpha,alpha-trehalose + CoA
show the reaction diagram
-
-
-
?
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2.5
2-O-sulfo-alpha,alpha-trehalose
pH 7.5, 25°C
0.006
palmitoyl-CoA
pH 7.5, 25°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0067
2-O-sulfo-alpha,alpha-trehalose
pH 7.5, 25°C
0.0032
palmitoyl-CoA
pH 7.5, 25°C
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
molecular modeling of structure
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D170A
catalytically inactive
H166A
catalytically inactive
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Tahir, R.; Sehgal, S.; Ijaz, A.
In silico comparative modeling of PapA1 and PapA2 proteins involved in Mycobacterium tuberculosis sulfolipid-1 biosynthesis pathway
Int. J. Bioautomation
16
155-164
2012
Mycobacterium tuberculosis (P9WIK7), Mycobacterium tuberculosis H37Rv (P9WIK7)
-
Manually annotated by BRENDA team
Seeliger, J.C.; Holsclaw, C.M.; Schelle, M.W.; Botyanszki, Z.; Gilmore, S.A.; Tully, S.E.; Niederweis, M.; Cravatt, B.F.; Leary, J.A.; Bertozzi, C.R.
Elucidation and chemical modulation of sulfolipid-1 biosynthesis in Mycobacterium tuberculosis
J. Biol. Chem.
287
7990-8000
2012
Mycobacterium tuberculosis (P9WIK7), Mycobacterium tuberculosis ATCC 25618 (P9WIK7)
Manually annotated by BRENDA team
Bhatt, K.; Gurcha, S.S.; Bhatt, A.; Besra, G.S.; Jacobs, W.R.
Two polyketide-synthase-associated acyltransferases are required for sulfolipid biosynthesis in Mycobacterium tuberculosis
Microbiology
153
513-520
2007
Mycobacterium tuberculosis (P9WIK7), Mycobacterium tuberculosis, Mycobacterium tuberculosis ATCC 25618 (P9WIK7)
Manually annotated by BRENDA team
Kumar, P.; Schelle, M.W.; Jain, M.; Lin, F.L.; Petzold, C.J.; Leavell, M.D.; Leary, J.A.; Cox, J.S.; Bertozzi, C.R.
PapA1 and PapA2 are acyltransferases essential for the biosynthesis of the Mycobacterium tuberculosis virulence factor sulfolipid-1
Proc. Natl. Acad. Sci. USA
104
11221-11226
2007
Mycobacterium tuberculosis (P9WIK7), Mycobacterium tuberculosis ATCC 25618 (P9WIK7)
Manually annotated by BRENDA team