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Literature summary for 2.7.3.2 extracted from

  • Jourden, M.J.; Geiss, P.R.; Thomenius, M.J.; Horst, L.A.; Barty, M.M.; Brym, M.J.; Mulligan, G.B.; Almeida, R.M.; Kersteen, B.A.; Myers, N.R.; Snider, M.J.; Borders, C.L., Jr.; Edmiston, P.L.
    Transition state stabilization by six arginines clustered in the active site of creatine kinase (2005), Biochim. Biophys. Acta, 1751, 178-183.
    View publication on PubMed
Search for more literature for 2.7.3.2

Cloned(Commentary)

Cloned (Comment) Organism
expression of soluble wild-type and mutant enzymes in Escherichia coli strain BL21(DE3) Oryctolagus cuniculus

Protein Variants

Protein Variants Comment Organism
R129A site-directed mutagenesis, inactive mutant Oryctolagus cuniculus
R129K site-directed mutagenesis, very highly reduced activity compared to the wild-type enzyme Oryctolagus cuniculus
R131A site-directed mutagenesis, inactive mutant Oryctolagus cuniculus
R131K site-directed mutagenesis, reduced activity compared to the wild-type enzyme Oryctolagus cuniculus
R235A site-directed mutagenesis, inactive mutant Oryctolagus cuniculus
R235K site-directed mutagenesis, highly reduced activity compared to the wild-type enzyme Oryctolagus cuniculus
R291K site-directed mutagenesis, highly reduced activity compared to the wild-type enzyme Oryctolagus cuniculus
R319K site-directed mutagenesis, reduced activity compared to the wild-type enzyme Oryctolagus cuniculus
R340A site-directed mutagenesis, highly reduced activity compared to the wild-type enzyme Oryctolagus cuniculus
R340K site-directed mutagenesis, reduced activity compared to the wild-type enzyme Oryctolagus cuniculus
R340Q site-directed mutagenesis, highly reduced activity compared to the wild-type enzyme Oryctolagus cuniculus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information kinetics of wild-type and mutant enzymes Oryctolagus cuniculus
0.7
-
 ATP pH 9.0, 30°C, recombinant wild-type enzyme Oryctolagus cuniculus
0.7
-
 ATP ATP in form of MgATP2- Oryctolagus cuniculus
1.1
-
 ATP pH 9.0, 30°C, recombinant mutant R340K Oryctolagus cuniculus
1.1
-
 ATP ATP in form of MgATP2- Oryctolagus cuniculus
1.6
-
 ATP pH 9.0, 30°C, recombinant mutant R291K Oryctolagus cuniculus
1.6
-
 ATP pH 9.0, 30°C, recombinant mutant R340A Oryctolagus cuniculus
1.6
-
 ATP ATP in form of MgATP2- Oryctolagus cuniculus
3.6
-
 ATP pH 9.0, 30°C, recombinant mutant R235K Oryctolagus cuniculus
3.6
-
 ATP ATP in form of MgATP2- Oryctolagus cuniculus
7.3
-
 ATP pH 9.0, 30°C, recombinant mutant R340Q Oryctolagus cuniculus
7.3
-
 ATP ATP in form of MgATP2- Oryctolagus cuniculus
8.2
-
 Creatine pH 9.0, 30°C, recombinant mutant R340A Oryctolagus cuniculus
9
-
 Creatine pH 9.0, 30°C, recombinant wild-type enzyme Oryctolagus cuniculus
10.3
-
 ATP pH 9.0, 30°C, recombinant mutant R129A Oryctolagus cuniculus
10.3
-
 ATP ATP in form of MgATP2- Oryctolagus cuniculus
19
-
 Creatine pH 9.0, 30°C, recombinant mutant R340K Oryctolagus cuniculus
72
-
 Creatine pH 9.0, 30°C, recombinant mutant R235K Oryctolagus cuniculus
76
-
 Creatine pH 9.0, 30°C, recombinant mutant R291K Oryctolagus cuniculus
163
-
 Creatine pH 9.0, 30°C, recombinant mutant R340Q Oryctolagus cuniculus
167
-
 Creatine pH 9.0, 30°C, recombinant mutant R129A Oryctolagus cuniculus

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ MgATP2-, at 1 mM, dissociation constants of wild-type and mutant enzymes Oryctolagus cuniculus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + creatine Oryctolagus cuniculus key enzyme in energy homeostasis ADP + phosphocreatine
-
 r

Organism

Organism UniProt Comment Textmining
Oryctolagus cuniculus
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant wild-type and mutant enzymes from Escherichia coli strain Bl21(DE3) Oryctolagus cuniculus

Reaction

Reaction Comment Organism Reaction ID
ATP + creatine = ADP + phosphocreatine bireactant catalytic mechanism, transition state stabilization by six arginines clustered in the active site of the enzyme Oryctolagus cuniculus
a

Source Tissue

Source Tissue Comment Organism Textmining
skeletal muscle
-
 Oryctolagus cuniculus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + creatine
-
 Oryctolagus cuniculus ADP + phosphocreatine
-
 r
ATP + creatine key enzyme in energy homeostasis Oryctolagus cuniculus ADP + phosphocreatine
-
 r

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
 assay at Oryctolagus cuniculus

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.08
-
 ATP pH 9.0, 30°C, recombinant mutant R129A Oryctolagus cuniculus
0.08
-
 Creatine pH 9.0, 30°C, recombinant mutant R129A Oryctolagus cuniculus
0.08
-
 ATP ATP in form of MgATP2- Oryctolagus cuniculus
0.54
-
 ATP pH 9.0, 30°C, recombinant mutant R235K Oryctolagus cuniculus
0.54
-
 Creatine pH 9.0, 30°C, recombinant mutant R235K Oryctolagus cuniculus
0.54
-
 ATP ATP in form of MgATP2- Oryctolagus cuniculus
1.33
-
 ATP pH 9.0, 30°C, recombinant mutant R340Q Oryctolagus cuniculus
1.33
-
 Creatine pH 9.0, 30°C, recombinant mutant R340Q Oryctolagus cuniculus
1.33
-
 ATP ATP in form of MgATP2- Oryctolagus cuniculus
2.14
-
 ATP pH 9.0, 30°C, recombinant mutant R340A Oryctolagus cuniculus
2.14
-
 Creatine pH 9.0, 30°C, recombinant mutant R340A Oryctolagus cuniculus
2.14
-
 ATP ATP in form of MgATP2- Oryctolagus cuniculus
2.18
-
 ATP pH 9.0, 30°C, recombinant mutant R291K Oryctolagus cuniculus
2.18
-
 Creatine pH 9.0, 30°C, recombinant mutant R291K Oryctolagus cuniculus
2.18
-
 ATP ATP in form of MgATP2- Oryctolagus cuniculus
50.1
-
 ATP pH 9.0, 30°C, recombinant mutant R340K Oryctolagus cuniculus
50.1
-
 Creatine pH 9.0, 30°C, recombinant mutant R340K Oryctolagus cuniculus
50.1
-
 ATP ATP in form of MgATP2- Oryctolagus cuniculus
148
-
 ATP pH 9.0, 30°C, recombinant wild-type enzyme Oryctolagus cuniculus
148
-
 Creatine pH 9.0, 30°C, recombinant wild-type enzyme Oryctolagus cuniculus
148
-
 ATP ATP in form of MgATP2- Oryctolagus cuniculus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
9
-
 assay at Oryctolagus cuniculus

Cofactor

Cofactor Comment Organism Structure
ADP MgADP2- Oryctolagus cuniculus
ATP MgATP2- Oryctolagus cuniculus