Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Hatzios, S.K.; Schelle, M.W.; Holsclaw, C.M.; Behrens, C.R.; Botyanszki, Z.; Lin, F.L.; Carlson, B.L.; Kumar, P.; Leary, J.A.; Bertozzi, C.R.
    PapA3 is an acyltransferase required for polyacyltrehalose biosynthesis in Mycobacterium tuberculosis (2009), J. Biol. Chem., 284, 12745-12751 .
    View publication on PubMedView publication on EuropePMC

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.3.1.278 51809
-
mass spectrometry Mycobacterium tuberculosis
2.3.1.279 51809
-
mass spectrometry Mycobacterium tuberculosis

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.3.1.278 a mycolipenoyl-CoA + a 2-(long-chain-fatty acyl)-trehalose Mycobacterium tuberculosis the enzyme participates in the biosynthesis of polyacyltrehalose, a pentaacylated, trehalose-based glycolipid found in the cell wall of pathogenic strains a 2-(long-chain-fatty acyl)-3-mycolipenoyl-trehalose + CoA
-
?
2.3.1.278 a mycolipenoyl-CoA + a 2-(long-chain-fatty acyl)-trehalose Mycobacterium tuberculosis H37Rv the enzyme participates in the biosynthesis of polyacyltrehalose, a pentaacylated, trehalose-based glycolipid found in the cell wall of pathogenic strains a 2-(long-chain-fatty acyl)-3-mycolipenoyl-trehalose + CoA
-
?
2.3.1.279 a long-chain-fatty acyl-CoA + alpha,alpha-trehalose Mycobacterium tuberculosis the enzyme participates in the biosynthesis of polyacyltrehalose, a pentaacylated, trehalose-based glycolipid found in the cell wall of pathogenic strains a 2-(long-chain-fatty acyl)-trehalose + CoA
-
?
2.3.1.279 a long-chain-fatty acyl-CoA + alpha,alpha-trehalose Mycobacterium tuberculosis H37Rv the enzyme participates in the biosynthesis of polyacyltrehalose, a pentaacylated, trehalose-based glycolipid found in the cell wall of pathogenic strains a 2-(long-chain-fatty acyl)-trehalose + CoA
-
?

Organism

EC Number Organism UniProt Comment Textmining
2.3.1.278 Mycobacterium tuberculosis P9WIK5
-
-
2.3.1.278 Mycobacterium tuberculosis H37Rv P9WIK5
-
-
2.3.1.279 Mycobacterium tuberculosis P9WIK5
-
-
2.3.1.279 Mycobacterium tuberculosis H37Rv P9WIK5
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.3.1.278 expression in Escherichia coli BL21(DE3) Mycobacterium tuberculosis
2.3.1.279 expression in Escherichia coli BL21(DE3) Mycobacterium tuberculosis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.3.1.278 a mycolipenoyl-CoA + a 2-(long-chain-fatty acyl)-trehalose the enzyme participates in the biosynthesis of polyacyltrehalose, a pentaacylated, trehalose-based glycolipid found in the cell wall of pathogenic strains Mycobacterium tuberculosis a 2-(long-chain-fatty acyl)-3-mycolipenoyl-trehalose + CoA
-
?
2.3.1.278 a mycolipenoyl-CoA + a 2-(long-chain-fatty acyl)-trehalose the enzyme catalyses two successive activities. It first transfers an acyl (often palmitoyl) group to position 2 (see EC 2.3.1.279, long-chain-acyl-CoA-trehalose acyltransferase), followed by the transfer of a mycolipenyl group to position 3 Mycobacterium tuberculosis a 2-(long-chain-fatty acyl)-3-mycolipenoyl-trehalose + CoA
-
?
2.3.1.278 a mycolipenoyl-CoA + a 2-(long-chain-fatty acyl)-trehalose the enzyme participates in the biosynthesis of polyacyltrehalose, a pentaacylated, trehalose-based glycolipid found in the cell wall of pathogenic strains Mycobacterium tuberculosis H37Rv a 2-(long-chain-fatty acyl)-3-mycolipenoyl-trehalose + CoA
-
?
2.3.1.278 a mycolipenoyl-CoA + a 2-(long-chain-fatty acyl)-trehalose the enzyme catalyses two successive activities. It first transfers an acyl (often palmitoyl) group to position 2 (see EC 2.3.1.279, long-chain-acyl-CoA-trehalose acyltransferase), followed by the transfer of a mycolipenyl group to position 3 Mycobacterium tuberculosis H37Rv a 2-(long-chain-fatty acyl)-3-mycolipenoyl-trehalose + CoA
-
?
2.3.1.279 a long-chain-fatty acyl-CoA + alpha,alpha-trehalose the enzyme participates in the biosynthesis of polyacyltrehalose, a pentaacylated, trehalose-based glycolipid found in the cell wall of pathogenic strains Mycobacterium tuberculosis a 2-(long-chain-fatty acyl)-trehalose + CoA
-
?
2.3.1.279 a long-chain-fatty acyl-CoA + alpha,alpha-trehalose the enzyme catalyses two successive activities. It first transfers an acyl (often palmitoyl) group to position 2, followed by the transfer of a mycolipenyl group to position 3 (see EC 2.3.1.278, mycolipenoyl-CoA-2-(long-chain-fatty acyl)-trehalose mycolipenoyltransferase) Mycobacterium tuberculosis a 2-(long-chain-fatty acyl)-trehalose + CoA
-
?
2.3.1.279 a long-chain-fatty acyl-CoA + alpha,alpha-trehalose the enzyme participates in the biosynthesis of polyacyltrehalose, a pentaacylated, trehalose-based glycolipid found in the cell wall of pathogenic strains Mycobacterium tuberculosis H37Rv a 2-(long-chain-fatty acyl)-trehalose + CoA
-
?
2.3.1.279 a long-chain-fatty acyl-CoA + alpha,alpha-trehalose the enzyme catalyses two successive activities. It first transfers an acyl (often palmitoyl) group to position 2, followed by the transfer of a mycolipenyl group to position 3 (see EC 2.3.1.278, mycolipenoyl-CoA-2-(long-chain-fatty acyl)-trehalose mycolipenoyltransferase) Mycobacterium tuberculosis H37Rv a 2-(long-chain-fatty acyl)-trehalose + CoA
-
?

Synonyms

EC Number Synonyms Comment Organism
2.3.1.278 papA3
-
Mycobacterium tuberculosis
2.3.1.279 papA3
-
Mycobacterium tuberculosis

General Information

EC Number General Information Comment Organism
2.3.1.278 malfunction disruption of the papA3 gene from Mycobacterium tuberculosis results in the loss of polyacyltrehalose from bacterial lipid extracts Mycobacterium tuberculosis
2.3.1.278 metabolism the enzyme participates in the biosynthesis of polyacyltrehalose, a pentaacylated, trehalose-based glycolipid found in the cell wall of pathogenic strains Mycobacterium tuberculosis
2.3.1.279 malfunction disruption of the papA3 gene from Mycobacterium tuberculosis results in the loss of polyacyltrehalose from bacterial lipid extracts Mycobacterium tuberculosis
2.3.1.279 metabolism the enzyme participates in the biosynthesis of polyacyltrehalose, a pentaacylated, trehalose-based glycolipid found in the cell wall of pathogenic strains Mycobacterium tuberculosis