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Literature summary for 7.3.2.1 extracted from

  • Gupta, S.; Chakraborti, P.K.; Sarkar, D.
    Nucleotide-induced conformational change in the catalytic subunit of the phosphate-specific transporter from M. tuberculosis: implications for the ATPase structure (2005), Biochim. Biophys. Acta, 1750, 112-121.
    View publication on PubMed
Search for more literature for 7.3.2.1

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane
-
 Mycobacterium tuberculosis 16020
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Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + H2O + phosphate/out Mycobacterium tuberculosis the enzyme performs phosphate uptake energized by ATP hydrolysis ADP + phosphate + phosphate/in
-
 ?

Organism

Organism UniProt Comment Textmining
Mycobacterium tuberculosis
-
 gene pstB
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + H2O + phosphate/out the enzyme performs phosphate uptake energized by ATP hydrolysis Mycobacterium tuberculosis ADP + phosphate + phosphate/in
-
 ?
ATP + H2O + phosphate/out conformational and structural changes upon nucleotide binding analysis, overview Mycobacterium tuberculosis ADP + phosphate + phosphate/in
-
 ?

Subunits

Subunits Comment Organism
More tertiary structure of PstB, conformational and structural changes upon nucleotide binding analysis, structure modeling, overview Mycobacterium tuberculosis

Synonyms

Synonyms Comment Organism
More the enzyme belongs to the PstB-like ABC-family of permeases Mycobacterium tuberculosis
phosphate-specific transporter
-
 Mycobacterium tuberculosis
PstB
-
 Mycobacterium tuberculosis