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Literature summary for 1.7.1.7 extracted from

  • Smith, S.; Boitz, J.; Chidambaram, E.S.; Chatterjee, A.; Ait-Tihyaty, M.; Ullman, B.; Jardim, A.
    The cystathionine-beta-synthase domains on the guanosine 5'-monophosphate reductase and inosine 5'-monophosphate dehydrogenase enzymes from Leishmania regulate enzymatic activity in response to guanylate and adenylate nucleotide levels (2016), Mol. Microbiol., 100, 824-840 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
gene LMJF_17_0725, DNA and amino acid sequence determination and analysis, , the gene has a 131 amino acid insertion encoding two tandem CBS domains, sequence comparisons, recombinant expression in Escherichia coli strain H1174 Leishmania major

Inhibitors

Inhibitors Comment Organism Structure
IMP competitive versus GMP Leishmania major
Mycophenolic acid competitive versus NADPH Leishmania major

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information steady-state kinetic analysis Leishmania major

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
GMP + NADPH + H+ Leishmania major
-
IMP + NH3 + NADP+
-
?

Organism

Organism UniProt Comment Textmining
Leishmania major Q4QEB3
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant untagged enzyme from Escherichia coli strain H1174 by affinity chromatography Leishmania major

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
GMP + NADPH + H+
-
Leishmania major IMP + NH3 + NADP+
-
?
GMP + NADPH + H+ reductive deamination of GMP, the back conversion of IMP to GMP is highly unfavorable Leishmania major IMP + NH3 + NADP+
-
?
additional information enzyme nucleotide bindng analysis, nucleotide binding alters the quarternary structure of the enzyme, overview Leishmania major ?
-
?

Subunits

Subunits Comment Organism
More quaternary structure determination, LmGMPR subunits may adopt conformations with Trp121 differentially exposed to the aqueous environment Leishmania major

Synonyms

Synonyms Comment Organism
GMPR
-
Leishmania major
guanosine 5'-monophosphate reductase
-
Leishmania major
LmGMPR
-
Leishmania major
Lmj17.0725
-
Leishmania major
LMJF_17_0725
-
Leishmania major

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
assay at Leishmania major

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6.9
-
assay at Leishmania major

Cofactor

Cofactor Comment Organism Structure
additional information no activity with NADH Leishmania major
NADPH binding analysis Leishmania major

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.014
-
IMP pH 6.9, 25°C, recombinant enzyme Leishmania major
0.02
-
Mycophenolic acid pH 6.9, 25°C, recombinant enzyme Leishmania major

General Information

General Information Comment Organism
malfunction loss of the cystathionine-beta-synthase, CBS, domain may impair the catalytic activity of mutant lmgmprDELTACBS and/or cause a disruption of the protein structure Leishmania major
additional information LmGMPR subunits may adopt conformations with Trp121 differentially exposed to the aqueous environment, binding of ATP resulted in an emission spectrum with a lambdamax centered at 350 nm indicative of a conformational change that position Trp121 into a more solvent exposed environment Leishmania major
physiological function the cystathionine-beta-synthase domains on the guanosine 5-monophosphate reductase regulates the enzymatic activity in response to guanylate nucleotide levels. Recombinant enzyme LmGMPR complements the DELTAguaC mutation in Escherichia coli strain H1174 lacking bacterial GMPR Leishmania major