The enzyme, found in a number of bacterial strains, is a non-ribosomal peptide synthase (NRPS). The enzyme forms 3-amino-1,5-dihydropyridine-2,6-dione, which undergoes spontaneous oxidation to form the blue pigment indigoidine.
The enzyme appears in viruses and cellular organisms
The enzyme, found in a number of bacterial strains, is a non-ribosomal peptide synthase (NRPS). The enzyme forms 3-amino-1,5-dihydropyridine-2,6-dione, which undergoes spontaneous oxidation to form the blue pigment indigoidine.
Substrates: the Ox domain of indigoidine synthase utilizes an active-site base residue, tyrosine 665, to deprotonate a protein-bound L-glutaminyl residue Products: -
the enzyme is involved in indigoidine biosynthesis. In the wild-type background, indC expression is very low. This low expression is probably responsible for the absence of indigoidine production in the wild-type strain. The expression of indC is increased by a factor of about 2000 in the pecS mutant
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
in the wild-type background, indC expression is very low. This low expression is probably responsible for the absence of indigoidine production in the wild-type strain. The expression of indC is increased by a factor of about 2000 in the pecS mutant
indigoidine synthetase BpsA provides a colorimetric ATP assay that can be adapted to quantify the substrate preferences of other non-ribosomal peptide synthetase enzymes
development of a high throughput, colourimetric screen that monitors the phosphopantetheinyl transferase-mediated activation of the non-ribosomal peptide synthetase BpsA to a blue pigment (indigoidine) synthesising form in vitro. The BpsA assay can be applied to quantify the level of inhibition of phosphopantetheinyl transferase (an essential enzyme and drug target in Mycobacterium tuberculosis) and generate consistent EC50 data
Brown, A.; Owen, J.; Jung, J.; Baker, E.; Ackerley, D.
Inhibition of indigoidine synthesis as a high-throughput colourimetric screen for antibiotics targeting the essential Mycobacterium tuberculosis phosphopantetheinyl transferase pptt