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

BRENDA support

Literature summary for 2.7.3.3 extracted from

  • Yano, D.; Mimura, S.; Uda, K.; Suzuki, T.
    Arginine kinase from Myzostoma cirriferum, a basal member of annelids (2016), Comp. Biochem. Physiol. B, 198, 73-78.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, recombinant expression of C-terminally His6-tagged enzyme in Escherichia coli strain BL21 Myzostoma cirriferum

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information bisubstrate kinetics and binary dissociation constants, overview Myzostoma cirriferum

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Myzostoma cirriferum

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
33000
-
His-tagged recombinant enzyme, gel filtration Myzostoma cirriferum
37000
-
-
Myzostoma cirriferum
39600
-
-
Myzostoma cirriferum

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + L-arginine Myzostoma cirriferum
-
ADP + Nomega-phospho-L-arginine
-
r

Organism

Organism UniProt Comment Textmining
Myzostoma cirriferum
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant C-terminally His6-tagged enzyme from Escherichia coli strain BL21 by nickel affinity chromatography Myzostoma cirriferum

Reaction

Reaction Comment Organism Reaction ID
ATP + L-arginine = ADP + Nomega-phospho-L-arginine the two-substrate AK kinetics is explained by a random-order, rapid-equilibrium, kinetic mechanism Myzostoma cirriferum

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + L-arginine
-
Myzostoma cirriferum ADP + Nomega-phospho-L-arginine
-
r
ATP + L-arginine the enzyme is highly specific for L-arginine, reversible transfer of phosphate Myzostoma cirriferum ADP + Nomega-phospho-L-arginine
-
r

Subunits

Subunits Comment Organism
monomer 1 * 39600, about, sequence calculation, 1 * 37000, His-tagged recombinant enzyme, SDS-PAGE Myzostoma cirriferum

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
assay at Myzostoma cirriferum

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
38.9
-
ATP pH 7.5, 25°C, recombinant enzyme Myzostoma cirriferum
38.9
-
L-arginine pH 7.5, 25°C, recombinant enzyme Myzostoma cirriferum

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
assay at Myzostoma cirriferum

Cofactor

Cofactor Comment Organism Structure
ATP
-
Myzostoma cirriferum

General Information

General Information Comment Organism
evolution phylogenetic analysis of amino acid sequences of phosphagen kinases indicate that the Myzostoma AK gene lineage differs from that of the polychaete Sabellastarte spectabilis AK, which is a dimer of creatine kinase (CK) origin. It is likely that the Myzostoma AK gene lineage was lost at an early stage of annelid evolution and that Sabellastarte AK evolved secondarily from the CK gene. Analysis of evolution of phosphagen kinases of annelids with marked diversity, overview Myzostoma cirriferum