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Literature summary for 2.3.1.122 extracted from

  • Hiromasa, Y.; Yan, X.; Roche, T.E.
    Specific ion influences on self-association of pyruvate dehydrogenase kinase isoform 2 (PDHK2), binding of PDHK2 to the L2 lipoyl domain, and effects of the lipoyl group-binding site inhibitor, Nov3r (2008), Biochemistry, 47, 2312-2324.
    View publication on PubMed
Search for more literature for 2.3.1.122

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli as a His-tagged fusion protein Mycobacterium avium
expressed in Escherichia coli as a His-tagged fusion protein Mycobacterium leprae

Protein Variants

Protein Variants Comment Organism
L130S leucine at position 130 of Mycobacterium leprae FbpA limits access of mycolate-containing glycolipid substrates to their binding site. Mutant L130S exhibits an enhanced mycosyltransferase activity compared to wild-type while the ability to transfer the unbranched acyl chain is unchanged. Km (substrate: short-chain trehalose monomycolate): 0.043 mM, sharply decreased compared to wild-type Mycobacterium leprae
S130L mutant S130L of Mycobacterium avium exhibits a reduced mycosyltransferase activity compared to wild-type Mycobacterium avium

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.043
-
 alpha,alpha-trehalose 6-monomycolate mutant L130S, short-chain trehalose monomycolate is used as a substrate, Vmax: 4.27 nmol/min/nmol Mycobacterium leprae
0.459
-
 alpha,alpha-trehalose 6-monomycolate wild-type, short-chain trehalose monomycolate is used as a substrate, Vmax: 3.83 nmol/min/nmol Mycobacterium leprae

Organism

Organism UniProt Comment Textmining
Mycobacterium avium
-
-
-
Mycobacterium leprae
-
-
-

Purification (Commentary)

Purification (Comment) Organism
using Ni-NTA chromatography Mycobacterium avium
using Ni-NTA chromatography Mycobacterium leprae

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
 compared to FbpA of Mycobacterium leprae activity of FbpA is strikingly enhanced in Mycobacterium avium Mycobacterium avium
additional information
-
 compared to FbpA of Mycobacterium tuberculosis and Mycobacterium avium activity of FbpA is reduced in Mycobacterium leprae Mycobacterium leprae

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2 alpha,alpha-trehalose 6-monomycolate
-
 Mycobacterium avium alpha,alpha-trehalose 6,6'-dimycolate + alpha,alpha-trehalose
-
 ?
2 alpha,alpha-trehalose 6-monomycolate substrate contains alpha-branched long-chain fatty acids. Only tiny amounts of trehalose dimycolate are detected. It is shown that FbpA mycolyltransferase from Mycobacterium leprae retains the ability to transfer unbranched but not alpha-branched fatty acids Mycobacterium leprae alpha,alpha-trehalose 6,6'-dimycolate + alpha,alpha-trehalose
-
 ?
alpha,alpha-trehalose monomycolate + D-glucose D-glucose is used as an alternative acceptor substrate. FbpA mycolyltransferase from Mycobacterium leprae shows only trace of glucose monomycolate is detected Mycobacterium leprae D-glucose monomycolate + alpha,alpha-trehalose
-
 ?
alpha,alpha-trehalose monomycolate + D-glucose Mycobacterium tuberculosis and Mycobacterium avium, replace TDM with glucose monomycolate by borrowing host-derived glucose as an alternative substrate for the FbpA mycolyltransferase Mycobacterium avium D-glucose monomycolate + alpha,alpha-trehalose
-
 ?

Synonyms

Synonyms Comment Organism
FbpA mycolyltransferase
-
 Mycobacterium avium
FbpA mycolyltransferase
-
 Mycobacterium leprae

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
 assay at Mycobacterium avium
37
-
 assay at Mycobacterium leprae

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
 assay at Mycobacterium avium
7.5
-
 assay at Mycobacterium leprae