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Literature summary 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)

EC Number Cloned (Comment) Organism
2.7.7.3 expressed in Escherichia coli Mycobacterium tuberculosis

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.7.7.3 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

EC Number Inhibitors Comment Organism Structure
2.7.7.3 coenzyme A
-
 Mycobacterium tuberculosis

Organism

EC Number Organism UniProt Comment Textmining
2.7.7.3 Mycobacterium tuberculosis
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.7.7.3
-
 Mycobacterium tuberculosis

Substrates and Products (Substrate)

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

Subunits

EC Number Subunits Comment Organism
2.7.7.3 homohexamer x-ray crystallography Mycobacterium tuberculosis

Synonyms

EC Number Synonyms Comment Organism
2.7.7.3 phosphopantetheine adenylyltransferase
-
 Mycobacterium tuberculosis
2.7.7.3 PPAT
-
 Mycobacterium tuberculosis

General Information

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