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Literature summary for 2.7.7.3 extracted from

  • Wubben, T.; Mesecar, A.D.
    Structure of Mycobacterium tuberculosis phosphopantetheine adenylyltransferase in complex with the feedback inhibitor CoA reveals only one active-site conformation (2011), Acta Crystallogr. Sect. F, 67, 541-545.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli Mycobacterium tuberculosis

Crystallization (Commentary)

Crystallization (Comment) Organism
in complex with coenzyme A, hanging drop vapor diffusion method, using 0.1 M Tris base pH 8.0 and 0.15 M magnesium formate Mycobacterium tuberculosis

Inhibitors

Inhibitors Comment Organism Structure
coenzyme A
-
Mycobacterium tuberculosis

Organism

Organism UniProt Comment Textmining
Mycobacterium tuberculosis
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Mycobacterium tuberculosis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + pantetheine 4'-phosphate
-
Mycobacterium tuberculosis diphosphate + 3'-dephospho-CoA
-
r

Subunits

Subunits Comment Organism
homohexamer x-ray crystallography Mycobacterium tuberculosis

Synonyms

Synonyms Comment Organism
phosphopantetheine adenylyltransferase
-
Mycobacterium tuberculosis
PPAT
-
Mycobacterium tuberculosis

General Information

General Information Comment Organism
metabolism the enzyme catalyzes the penultimate step in the coenzyme A biosynthetic pathway Mycobacterium tuberculosis