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Literature summary for 2.7.11.7 extracted from

  • Szczepanowska, J.; Ramachandran, U.; Herring, C.J.; Gruschus, J.M.; Qin, J.; Korn, E.D.; Brzeska, H.
    Effect of mutating the regulatory phosphoserine and conserved threonine on the activity of the expressed catalytic domain of Acanthamoeba myosin I heavy chain kinase (1998), Proc. Natl. Acad. Sci. USA, 95, 4146-4151.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.7.11.7

Activating Compound

Activating Compound Comment Organism Structure
additional information
-
 Acanthamoeba castellanii

Cloned(Commentary)

Cloned (Comment) Organism
cloning of wild-type and mutants of the catalytic domain of myosin I heavy chain kinase as His-tagged proteins and expression in Spodoptera frugiperda Sf9 cells via baculovirus infection system Acanthamoeba castellanii

Protein Variants

Protein Variants Comment Organism
S627A catalytic domain mutant, mutation of potential phosphorylation site, no phosphorylation of the mutant, reduced activity, increased Km values for the substrates, but higher activity than the unphosphorylated wild-type enzyme Acanthamoeba castellanii
S627D catalytic domain mutant, mutation of potential phosphorylation site, no phosphorylation of the mutant, reduced activity, increased Km values for the substrates, the acidic residue cannot substitute for phospho-Ser Acanthamoeba castellanii
S627E catalytic domain mutant, mutation of potential phosphorylation site, no phosphorylation of the mutant, reduced activity, increased Km values for the substrates, the acidic residue cannot substitute for phospho-Ser Acanthamoeba castellanii
T631A catalytic domain mutant, mutation of a conserved Thr residue, full phosphorylation of the mutant, reduced activity, increased Km values for the substrates Acanthamoeba castellanii
T631D catalytic domain mutant, mutation of a conserved Thr residue, 95% phosphorylation of the mutant, highly reduced activity, increased Km values for the substrates Acanthamoeba castellanii
T631E catalytic domain mutant, mutation of a conserved Thr residue, no phosphorylation of the mutant, highly reduced activity, highly increased Km values for the substrates Acanthamoeba castellanii
T632A catalytic domain mutant, mutation of a nonconserved Thr residue, full phosphorylation of the mutant, increased activity, only slightly increased Km values for the substrates Acanthamoeba castellanii
T632D catalytic domain mutant, mutation of a nonconserved Thr residue, 80% phosphorylation of the mutant, reduced activity, increased Km values for the substrates Acanthamoeba castellanii
T632E catalytic domain mutant, mutation of a nonconserved Thr residue, full phosphorylation of the mutant, reduced activity, increased Km values for the substrates Acanthamoeba castellanii

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information catalytic domain mutants Acanthamoeba castellanii
0.15
-
 GRGRSSVYS recombinant wild-type catalytic domain, pH 7.0, 30°C Acanthamoeba castellanii
0.16
-
 ATP recombinant wild-type catalytic domain, pH 7.0, 30°C Acanthamoeba castellanii
0.2
-
 GRGRSSVYS recombinant T632A mutant catalytic domain, pH 7.0, 30°C Acanthamoeba castellanii
0.3
-
 ATP recombinant T632A mutant catalytic domain, pH 7.0, 30°C Acanthamoeba castellanii

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + myosin I heavy chain Acanthamoeba castellanii
-
 ADP + myosin I heavy chain phosphate
-
 ?

Organism

Organism UniProt Comment Textmining
Acanthamoeba castellanii
-
 myosin I heavy chain kinase
-

Purification (Commentary)

Purification (Comment) Organism
recombinant His-tagged catalytic domains, wild-type and mutants, from Sf9 insect cells Acanthamoeba castellanii

Reaction

Reaction Comment Organism Reaction ID
ATP + [myosin heavy-chain] = ADP + [myosin heavy-chain] phosphate catalytic domain structure, modeling Acanthamoeba castellanii
a
ATP + [myosin heavy-chain] = ADP + [myosin heavy-chain] phosphate residues Ser627, Thr631 and Thr632 are essential for catalytic activity Acanthamoeba castellanii
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + GRGRSSVYS synthetic peptide with a sequence corresponding to the phosphorylation site of myosin IC Acanthamoeba castellanii ADP + GRGRSS(-phosphate)VYS
-
 ?
ATP + myosin I heavy chain
-
 Acanthamoeba castellanii ADP + myosin I heavy chain phosphate
-
 ?

Synonyms

Synonyms Comment Organism
MIHCK
-
 Acanthamoeba castellanii

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
additional information
-
 additional information catalytic domain mutants Acanthamoeba castellanii
71
-
 GRGRSSVYS recombinant wild-type catalytic domain, pH 7.0, 30°C Acanthamoeba castellanii
105
-
 GRGRSSVYS recombinant T632A mutant catalytic domain, pH 7.0, 30°C Acanthamoeba castellanii

Cofactor

Cofactor Comment Organism Structure
ATP
-
 Acanthamoeba castellanii