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Literature summary for 6.3.5.2 extracted from

  • Bhat, J.Y.; Venkatachala, R.; Singh, K.; Gupta, K.; Sarma, S.P.; Balaram, H.
    Ammonia channeling in Plasmodium falciparum GMP synthetase: investigation by NMR spectroscopy and biochemical assays (2011), Biochemistry, 50, 3346-3356.
    View publication on PubMed
Search for more literature for 6.3.5.2

Cloned(Commentary)

Cloned (Comment) Organism
-
 Plasmodium falciparum

Protein Variants

Protein Variants Comment Organism
C102A totally devoid of glutamine-dependent activity. Kinetic constants for NH4Cl, ATP, and XMP obtained for the ammonia-dependent activity are similar to that of the wild-type enzyme Plasmodium falciparum

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.132
-
 NH3 pH 7.4, 25°C Plasmodium falciparum

Organism

Organism UniProt Comment Textmining
Plasmodium falciparum
-
-
-

Reaction

Reaction Comment Organism Reaction ID
ATP + XMP + L-glutamine + H2O = AMP + diphosphate + GMP + L-glutamate evidence for ammonia channeling. Ammonia released from glutamine is not equilibrated with the external medium. Saturating concentrations of glutamine do not obliterate the incorporation of external ammonia into GMP. Ammonia in the external medium can access the thioester intermediate when the ATPPase domain is bound to substrates Plasmodium falciparum
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + XMP + L-Gln enzyme can use both glutamine and external ammonia, the kinetic parameters kcat and Km for the two substrates are different and also exhibit a pH-dependent change Plasmodium falciparum AMP + diphosphate + GMP + L-Glu
-
 ?
ATP + XMP + NH3 enzyme can use both glutamine and external ammonia, the kinetic parameters kcat and Km for the two substrates are different and also exhibit a pH-dependent change Plasmodium falciparum AMP + diphosphate + GMP
-
 ?

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.66
-
 L-Gln pH 7.4, 25°C Plasmodium falciparum
0.933
-
 NH3 pH 7.4, 25°C Plasmodium falciparum

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.4
-
 glutamine-dependent activity Plasmodium falciparum
9.2
-
 ammonia-dependent activity Plasmodium falciparum