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Information on EC 2.3.1.283 - 2'-acyl-2-O-sulfo-trehalose (hydroxy)phthioceranyltransferase and Organism(s) Mycobacterium tuberculosis and UniProt Accession P9WIK9

for references in articles please use BRENDA:EC2.3.1.283
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IUBMB Comments
This mycobacterial enzyme catalyses the acylation of 2'-palmitoyl/stearoyl-2-O-sulfo-alpha,alpha-trehalose at the 3' position by a (hydroxy)phthioceranoyl group during the biosynthesis of mycobacterial sulfolipids.
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This record set is specific for:
Mycobacterium tuberculosis
UNIPROT: P9WIK9
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The taxonomic range for the selected organisms is: Mycobacterium tuberculosis
The expected taxonomic range for this enzyme is: Mycobacterium tuberculosis
Reaction Schemes
a (hydroxy)phthioceranyl-[(hydroxy)phthioceranic acid synthase]
+
2'-palmitoyl/stearoyl-2-O-sulfo-alpha,alpha-trehalose
=
a 3'-(hydroxy)phthioceranyl-2'-palmitoyl/stearoyl-2-O-sulfo-alpha,alpha-trehalose
+
holo-[(hydroxy)phthioceranic acid synthase]
Synonyms
papa1, rv3824c, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SL659 acyltransferase PapA1
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papA1
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PATHWAY SOURCE
PATHWAYS
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-
SYSTEMATIC NAME
IUBMB Comments
(hydroxy)phthioceranyl-[(hydroxy)phthioceranic acid synthase]:2'-acyl-2-O-sulfo-alpha,alpha-trehalose 3'-(hydroxy)phthioceranyltransferase
This mycobacterial enzyme catalyses the acylation of 2'-palmitoyl/stearoyl-2-O-sulfo-alpha,alpha-trehalose at the 3' position by a (hydroxy)phthioceranoyl 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
a (hydroxy)phthioceranyl-[(hydroxy)phthioceranic acid synthase] + 2'-palmitoyl/stearoyl-2-O-sulfo-alpha,alpha-trehalose
a 3'-(hydroxy)phthioceranyl-2'-palmitoyl/stearoyl-2-O-sulfo-alpha,alpha-trehalose + holo-[(hydroxy)phthioceranic acid synthase]
show the reaction diagram
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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
a (hydroxy)phthioceranyl-[(hydroxy)phthioceranic acid synthase] + 2'-palmitoyl/stearoyl-2-O-sulfo-alpha,alpha-trehalose
a 3'-(hydroxy)phthioceranyl-2'-palmitoyl/stearoyl-2-O-sulfo-alpha,alpha-trehalose + holo-[(hydroxy)phthioceranic acid synthase]
show the reaction diagram
-
-
-
?
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
homology modeling of protein and comparison of different homology modeling programs
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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
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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 (P9WIK9), Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv (P9WIK9)
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 (P9WIK9), Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv (P9WIK9)
Manually annotated by BRENDA team