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Literature summary for 2.7.7.3 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)

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

Crystallization (Commentary)

Crystallization (Comment) Organism
-
Mycobacterium tuberculosis

Natural Substrates/ Products (Substrates)

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

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

Subunits

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