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Literature summary extracted from

  • Gupta, S.; Yadav, S.; Singh, N.; Verma, A.; Siddiqi, I.; Saxena, J.K.
    Purification and characterization of guanylate kinase, a nucleoside monophosphate kinase of Brugia malayi (2014), Parasitology, 141, 1341-1352.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.7.4.8 DNA and amino acid sequence determination and analysis, phylogenetic tree, recombinant expression of C-terminally and N-terminally His-tagged enzyme in Escherichia coli BL21 (DE3) Brugia malayi

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.7.4.8 aurin 82% inhibition at 0.05 mM Brugia malayi
2.7.4.8 Ca2+ high inhibition at 1 mM Brugia malayi
2.7.4.8 EDTA complete inhibition at 1 mM Brugia malayi
2.7.4.8 additional information no or poor inhibition by sulfhydryl group inhibitors p-chloromercuribenzoate and N-ethylmaleimide, reducing agents (DTT and BME) and His modification by diethyl dicarbonate. No or poor inhibition by DEC, ivermectin and levamisole Brugia malayi
2.7.4.8 Ni2+ high inhibition at 1 mM Brugia malayi
2.7.4.8 PMSF inhibits 65% at 5 mM Brugia malayi
2.7.4.8 suramin 83.5% inhibition at 0.01 mM Brugia malayi
2.7.4.8 Zn2+ high inhibition at 1 mM Brugia malayi

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.7.4.8 0.03
-
 GMP pH 7.5, 25°C, recombinant enzyme Brugia malayi
2.7.4.8 0.038
-
 dGMP pH 7.5, 25°C, recombinant enzyme Brugia malayi

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.7.4.8 Mg2+ required Brugia malayi
2.7.4.8 Mn2+ can partially substitute for Mg2+ Brugia malayi

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.7.4.8 24000
-
-
 Brugia malayi
2.7.4.8 45000
-
 gel filtration Brugia malayi

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.7.4.8 ATP + GMP Brugia malayi
-
 ADP + GDP
-
 r

Organism

EC Number Organism UniProt Comment Textmining
2.7.4.8 Brugia malayi Q5GS56 gene GMK
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.7.4.8 recombinant His-tagged enzyme from Escherichia coli BL21 (DE3) by nickel affinity chromatography Brugia malayi

Reaction

EC Number Reaction Comment Organism Reaction ID
2.7.4.8 ATP + GMP = ADP + GDP sequential catalytic mechanism Brugia malayi
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.4.8 ATP + dGMP
-
 Brugia malayi ADP + dGDP
-
 r
2.7.4.8 ATP + GMP
-
 Brugia malayi ADP + GDP
-
 r
2.7.4.8 ATP + GMP GMP and ATP served as the most effective phosphate acceptor and donor, respectively Brugia malayi ADP + GDP
-
 r
2.7.4.8 dATP + GMP
-
 Brugia malayi dADP + GDP
-
 r
2.7.4.8 GTP + dAMP
-
 Brugia malayi GDP + dADP
-
 r
2.7.4.8 additional information recombinant enzyme BmGK utilizes both GMP and dGMP as substrates. No activity with dTMP, UMP, CMP, dCMP, IMP, XMP, CTP, UTP, and TTP Brugia malayi ?
-
 ?

Subunits

EC Number Subunits Comment Organism
2.7.4.8 homodimer 2 * 24000, SDS-PAGE, gel filtration and glutaraldehyde cross-linking Brugia malayi
2.7.4.8 More the secondary structure of BmGK consists of 45% alpha-helices, 18% beta-sheets, by circular dichrosim analysis Brugia malayi

Synonyms

EC Number Synonyms Comment Organism
2.7.4.8 ATP: GMP phosphotransferase
-
 Brugia malayi
2.7.4.8 BmGK
-
 Brugia malayi
2.7.4.8 guanosine monophosphate kinase
-
 Brugia malayi

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.7.4.8 40
-
-
 Brugia malayi

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
2.7.4.8 15 50 activity range, profile overview Brugia malayi

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2.7.4.8 510
-
 dGMP pH 7.5, 25°C, recombinant enzyme Brugia malayi
2.7.4.8 1500
-
 GMP pH 7.5, 25°C, recombinant enzyme Brugia malayi

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.7.4.8 7.5
-
-
 Brugia malayi

pH Range

EC Number pH Minimum pH Maximum Comment Organism
2.7.4.8 6 8 activity range, profile overview Brugia malayi

Cofactor

EC Number Cofactor Comment Organism Structure
2.7.4.8 ATP
-
 Brugia malayi

General Information

EC Number General Information Comment Organism
2.7.4.8 additional information free Mg+2 (not complexed to ATP) and GTP play a regulatory role in catalysis of BmGK. The enzyme shows a higher catalytic efficiency compared to the human enzyme and shows ternary complex (BmGK-GMP-ATP) formation with sequential substrate binding. Homology modelling and docking study with GMP using the crystal structure of the yeast enzyme, PDB ID 1EX7 Brugia malayi

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
2.7.4.8 13400
-
 GMP pH 7.5, 25°C, recombinant enzyme Brugia malayi
2.7.4.8 50000
-
 GMP pH 7.5, 25°C, recombinant enzyme Brugia malayi