Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 3.6.1.31 extracted from

  • Javid-Majd, F.; Yang, D.; Ioerger, T.R.; Sacchettini, J.C.
    The 1.25 A resolution structure of phosphoribosyl-ATP pyrophosphohydrolase from Mycobacterium tuberculosis (2008), Acta Crystallogr. Sect. D, 64, 627-635.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.6.1.31

Application

Application Comment Organism
drug development because of its essentiality for growth in vitro, HisE is a potential drug target for tuberculosis Mycobacterium tuberculosis

Crystallization (Commentary)

Crystallization (Comment) Organism
native and selenomethionine-labeled, uncomplexed enzyme in two crystal forms, hanging-drop vapor diffusion method, 10 mg/ml protein in 20 mM HEPES, pH 7.5, mixing of protein solution and reservoir buffer containing 100 mM sodium cacodylate pH 6.5, 1.0 M sodium citrate, 0.1 M guanidinium hydrochloride in a 1:1 ratio, 4 days, X-ray structure determination and analysis at 1.25 A and 1.79 A resolution, respectively Mycobacterium tuberculosis

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+
-
 Mycobacterium tuberculosis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1-(5-phosphoribosyl)-ATP + H2O Mycobacterium tuberculosis phosphoribosyl-ATP pyrophosphohydrolase is the second enzyme in the histidine-biosynthetic pathway, irreversibly hydrolyzing phosphoribosyl-ATP to phosphoribosyl-AMP and pyrophosphate 1-(5-phosphoribosyl)-AMP + diphosphate
-
 ir
1-(5-phosphoribosyl)-ATP + H2O Mycobacterium tuberculosis H37Rv phosphoribosyl-ATP pyrophosphohydrolase is the second enzyme in the histidine-biosynthetic pathway, irreversibly hydrolyzing phosphoribosyl-ATP to phosphoribosyl-AMP and pyrophosphate 1-(5-phosphoribosyl)-AMP + diphosphate
-
 ir
additional information Mycobacterium tuberculosis HisE essentiality for growth in vitro ?
-
 ?
additional information Mycobacterium tuberculosis H37Rv HisE essentiality for growth in vitro ?
-
 ?

Organism

Organism UniProt Comment Textmining
Mycobacterium tuberculosis P9WMM9 gene hisE
-
Mycobacterium tuberculosis H37Rv P9WMM9 gene hisE
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1-(5-phosphoribosyl)-ATP + H2O active site structure, overview Mycobacterium tuberculosis 1-(5-phosphoribosyl)-AMP + diphosphate
-
 ir
1-(5-phosphoribosyl)-ATP + H2O phosphoribosyl-ATP pyrophosphohydrolase is the second enzyme in the histidine-biosynthetic pathway, irreversibly hydrolyzing phosphoribosyl-ATP to phosphoribosyl-AMP and pyrophosphate Mycobacterium tuberculosis 1-(5-phosphoribosyl)-AMP + diphosphate
-
 ir
1-(5-phosphoribosyl)-ATP + H2O active site structure, overview Mycobacterium tuberculosis H37Rv 1-(5-phosphoribosyl)-AMP + diphosphate
-
 ir
1-(5-phosphoribosyl)-ATP + H2O phosphoribosyl-ATP pyrophosphohydrolase is the second enzyme in the histidine-biosynthetic pathway, irreversibly hydrolyzing phosphoribosyl-ATP to phosphoribosyl-AMP and pyrophosphate Mycobacterium tuberculosis H37Rv 1-(5-phosphoribosyl)-AMP + diphosphate
-
 ir
additional information HisE essentiality for growth in vitro Mycobacterium tuberculosis ?
-
 ?
additional information HisE essentiality for growth in vitro Mycobacterium tuberculosis H37Rv ?
-
 ?

Subunits

Subunits Comment Organism
homodimer the biological unit of the protein is a homodimer, with an active site on each subunit composed of residues exclusively from that subunit, the protein is composed of five alpha-helices with connecting loops Mycobacterium tuberculosis
More structure comparisons, overview Mycobacterium tuberculosis

Synonyms

Synonyms Comment Organism
HisE
-
 Mycobacterium tuberculosis
More the enzyme is a member of the alpha-helical nucleoside-triphosphate pyrophosphatase superfamily Mycobacterium tuberculosis
phosphoribosyl-ATP pyrophosphohydrolase
-
 Mycobacterium tuberculosis