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Literature summary extracted from

  • Morris, V.K.; Izard, T.
    Substrate-induced asymmetry and channel closure revealed by the apoenzyme structure of Mycobacterium tuberculosis phosphopantetheine adenylyltransferase (2004), Protein Sci., 13, 2547-2552.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.7.7.3 expressed in Escherichia coli BL21(DE3) Mycobacterium tuberculosis

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.7.7.3
-
 Mycobacterium tuberculosis

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.7.7.3 ATP + pantetheine 4'-phosphate Mycobacterium tuberculosis rate-limiting penultimate step in coenzyme A biosynthesis diphosphate + 3'-dephospho-CoA
-
 r

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
2.7.7.3 ATP + pantetheine 4'-phosphate rate-limiting penultimate step in coenzyme A biosynthesis Mycobacterium tuberculosis diphosphate + 3'-dephospho-CoA
-
 r

Subunits

EC Number Subunits Comment Organism
2.7.7.3 hexamer crystal structure analysis hexamer is composed of two identical trimers, ligand binding was found to alter the protein structure Mycobacterium tuberculosis