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

BRENDA support

Literature summary for 2.7.1.35 extracted from

  • Kumar, V.; Sharma, M.; Rakesh, B.R.; Malik, C.K.; Neelagiri, S.; Neerupudi, K.B.; Garg, P.; Singh, S.
    Pyridoxal kinase a vitamin B6 salvage pathway enzyme from Leishmania donovani (2018), Int. J. Biol. Macromol., 119, 320-334 .
    View publication on PubMed
Search for more literature for 2.7.1.35

Application

Application Comment Organism
drug development in silico analysis of the human and parasite PdxK structure reveals significant differences in the active site region thus highlighting the potential of the parasite PdxK as an antileishmanial drug target Leishmania donovani

Cloned(Commentary)

Cloned (Comment) Organism
gene pdxK, DNA and amino acid sequence determination and analysis, sequence comparisons, recombinant expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3), subcloning in Escherichia coli strain DH5alpha. LdPdxK-overexpressing parasites are generated by episomal expression of the enzyme Leishmania donovani

Protein Variants

Protein Variants Comment Organism
D231A site-directed mutagenesis of a GXGD motif residue, inactive mutant Leishmania donovani
G228A site-directed mutagenesis of a GXGD motif residue, inactive mutant Leishmania donovani
G230A site-directed mutagenesis of a GXGD motif residue, inactive mutant Leishmania donovani
T229A site-directed mutagenesis of a GXGD motif residue, the mutation does not affect the catalytic function of enzyme LdPdxK, mutant T229A shows enzyme activity almost similar to wild-type LdPdxK. The Km value of T229A mutant for pyridoxal is 1.6fold reduced and the Km increased compared to wild-type Leishmania donovani

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information Michaelis-Menten kinetics Leishmania donovani
0.2
-
 ATP recombinant wild-type enzyme, pH 7.2, 37°C Leishmania donovani
0.24
-
 pyridoxal recombinant wild-type enzyme, pH 7.2, 37°C Leishmania donovani

Localization

Localization Comment Organism GeneOntology No. Textmining
cytosol
-
 Leishmania donovani 5829
-

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ activates Leishmania donovani
Co2+ activates Leishmania donovani
Cu2+ activates slightly Leishmania donovani
Fe2+ activates Leishmania donovani
Mg2+ activates Leishmania donovani
Mn2+ activates Leishmania donovani
additional information the enzyme requires a metal cofactor, very low activity with Li+, Na+, K+, Rb+ and Cs+. Cobalt gives more activity when compared to that of Zn2+, Ca2+, Cu2+ and Ni2+. Cu2+ shows the least enzyme activity. Order of metal ions with increasing effect on enzyme activity is as follows: Co2+, Zn2+, Mn2+, Mg2+, Fe2+, Ca2+, Ni2+, Cu2+ Leishmania donovani
Ni2+ activates Leishmania donovani
Zn2+ activates Leishmania donovani

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + pyridoxal Leishmania donovani
-
 ADP + pyridoxal 5'-phosphate
-
 ?
ATP + pyridoxal Leishmania donovani MHOM/80/IN/Dd8
-
 ADP + pyridoxal 5'-phosphate
-
 ?

Organism

Organism UniProt Comment Textmining
Leishmania donovani A0A0G2YFI9
-
-
Leishmania donovani MHOM/80/IN/Dd8 A0A0G2YFI9
-
-

Source Tissue

Source Tissue Comment Organism Textmining
amastigote
-
 Leishmania donovani
-
promastigote
-
 Leishmania donovani
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1847
-
 purified recombinant His-tagged wild-type enzyme, pH 7.2, 37°C Leishmania donovani

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + pyridoxal
-
 Leishmania donovani ADP + pyridoxal 5'-phosphate
-
 ?
ATP + pyridoxal
-
 Leishmania donovani MHOM/80/IN/Dd8 ADP + pyridoxal 5'-phosphate
-
 ?

Subunits

Subunits Comment Organism
? x * 33000, recombinant His-tagged enzyme, SDS-PAGE Leishmania donovani
More native LdPdxK enzyme exhibits 43.3% alpha-helix, 24.8% beta-sheet, 0% turn, and 31.9% random coil content Leishmania donovani

Synonyms

Synonyms Comment Organism
LdPdxK
-
 Leishmania donovani
PdxK
-
 Leishmania donovani

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
42
-
 recombinant enzyme Leishmania donovani

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
25 42 maximal activity at 42°C, 80% of maximal activity at 37°C, 50% at 25°C, purified recombinant enzyme Leishmania donovani

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.02
-
 ATP recombinant wild-type enzyme, pH 7.2, 37°C Leishmania donovani
1.5
-
 pyridoxal recombinant wild-type enzyme, pH 7.2, 37°C Leishmania donovani

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.2
-
 assay at Leishmania donovani

General Information

General Information Comment Organism
additional information in silico analysis of the human and parasite PdxK structure revealing significant differences in the active site region, LdPdxK homology modeling using pyridoxal kinase from Trypanosoma brucei (PDB ID 3ZS7) as a template, molecular dynamics and molecular docking, overview Leishmania donovani
physiological function pyridoxal kinase (PdxK) is an important enzyme of the vitamin B6 salvage pathway which is required for phosphorylation of B6 vitamers Leishmania donovani

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
5.33
-
 ATP recombinant wild-type enzyme, pH 7.2, 37°C Leishmania donovani
6.25
-
 pyridoxal recombinant wild-type enzyme, pH 7.2, 37°C Leishmania donovani