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Literature summary extracted from

  • 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 (2007), Proc. Natl. Acad. Sci. USA, 104, 11221-11226 .
    View publication on PubMedView publication on EuropePMC

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.3.1.288 0.006
-
palmitoyl-CoA pH 7.5, 25°C Mycobacterium tuberculosis
2.3.1.288 2.5
-
2-O-sulfo-alpha,alpha-trehalose pH 7.5, 25°C Mycobacterium tuberculosis

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.3.1.283 a (hydroxy)phthioceranyl-[(hydroxy)phthioceranic acid synthase] + 2'-palmitoyl/stearoyl-2-O-sulfo-alpha,alpha-trehalose Mycobacterium tuberculosis
-
a 3'-(hydroxy)phthioceranyl-2'-palmitoyl/stearoyl-2-O-sulfo-alpha,alpha-trehalose + holo-[(hydroxy)phthioceranic acid synthase]
-
?
2.3.1.283 a (hydroxy)phthioceranyl-[(hydroxy)phthioceranic acid synthase] + 2'-palmitoyl/stearoyl-2-O-sulfo-alpha,alpha-trehalose Mycobacterium tuberculosis H37Rv
-
a 3'-(hydroxy)phthioceranyl-2'-palmitoyl/stearoyl-2-O-sulfo-alpha,alpha-trehalose + holo-[(hydroxy)phthioceranic acid synthase]
-
?

Organism

EC Number Organism UniProt Comment Textmining
2.3.1.283 Mycobacterium tuberculosis P9WIK9
-
-
2.3.1.283 Mycobacterium tuberculosis H37Rv P9WIK9
-
-
2.3.1.288 Mycobacterium tuberculosis P9WIK7
-
-
2.3.1.288 Mycobacterium tuberculosis ATCC 25618 P9WIK7
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.3.1.283 a (hydroxy)phthioceranyl-[(hydroxy)phthioceranic acid synthase] + 2'-palmitoyl/stearoyl-2-O-sulfo-alpha,alpha-trehalose
-
Mycobacterium tuberculosis a 3'-(hydroxy)phthioceranyl-2'-palmitoyl/stearoyl-2-O-sulfo-alpha,alpha-trehalose + holo-[(hydroxy)phthioceranic acid synthase]
-
?
2.3.1.283 a (hydroxy)phthioceranyl-[(hydroxy)phthioceranic acid synthase] + 2'-palmitoyl/stearoyl-2-O-sulfo-alpha,alpha-trehalose
-
Mycobacterium tuberculosis H37Rv a 3'-(hydroxy)phthioceranyl-2'-palmitoyl/stearoyl-2-O-sulfo-alpha,alpha-trehalose + holo-[(hydroxy)phthioceranic acid synthase]
-
?
2.3.1.288 palmitoyl-CoA + 2-O-sulfo-alpha,alpha-trehalose
-
Mycobacterium tuberculosis 2-O-sulfo-2'-palmitoyl-alpha,alpha-trehalose + CoA
-
?
2.3.1.288 palmitoyl-CoA + 2-O-sulfo-alpha,alpha-trehalose
-
Mycobacterium tuberculosis ATCC 25618 2-O-sulfo-2'-palmitoyl-alpha,alpha-trehalose + CoA
-
?

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2.3.1.288 0.0032
-
palmitoyl-CoA pH 7.5, 25°C Mycobacterium tuberculosis
2.3.1.288 0.0067
-
2-O-sulfo-alpha,alpha-trehalose pH 7.5, 25°C Mycobacterium tuberculosis

General Information

EC Number General Information Comment Organism
2.3.1.283 physiological function acyltransferases PapA2 and PapA1 are responsible for the sequential acylation of trehalose-2-sulfate to form diacylated intermediate sulfolipid SL1278 and are essential for sulfolipid-1 biosynthesis. In vitro, recombinant PapA2 converts of trehalose-2-sulfate to 2'-palmitoyl of trehalose-2-sulfate , and PapA1 further elaborates this SL-sulfolipid-1 intermediate to an analog of SL1278. PapA2 and PapA1 play an essential role in sulfolipid-1 biosynthesis . The loss of sulfolipid-1 (and SL1278) in Papa1 and Papa2 deletion mutants does not appear to affect bacterial replication or trafficking Mycobacterium tuberculosis
2.3.1.288 physiological function acyltransferases PapA2 and PapA1 are responsible for the sequential acylation of trehalose-2-sulfate to form diacetylated intermediate SL1278 and are essential for sulfolipid SL-1 biosynthesis. In vitro, recombinant PapA2 converts T2S to 2'-palmitoyl T2S, and PapA1 further elaborates this SL-1 intermediate to an analog of SL1278. Disruption of PapA2 and PapA1 genes results in loss of SL-1 (and SL1278). The deletions do not appear to affect bacterial replication, trafficking or virulence Mycobacterium tuberculosis