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Literature summary for 6.1.1.16 extracted from

  • Zhang, C.M.; Hou, Y.M.
    Domain-domain communication for tRNA aminoacylation: the importance of covalent connectivity (2005), Biochemistry, 44, 7240-7249.
    View publication on PubMed
Search for more literature for 6.1.1.16

Protein Variants

Protein Variants Comment Organism
C209S the ratio of turnover number to Km-value of aminoacylation of tRNACys is 0.0031% of the wild-type ratio Escherichia coli
C28S the ratio of turnover number to Km-value of aminoacylation of tRNACys is 0.012% of the wild-type ratio Escherichia coli
C28S/C209S the ratio of turnover number to Km-value of aminoacylation of tRNACys is 0.0026% of the wild-type ratio Escherichia coli
C28S/C209S/H234N/E238Q aminoacylation of tRNACys is not detectable Escherichia coli
DELTA288-461 the ratio of turnover number to Km-value for ATP in ATP-diphosphate exchange is 7% of the wild-type ratio Escherichia coli
DELTA328-461 the ratio of turnover number to Km-value for ATP in ATP-diphosphate exchange is 0.32% of the wild-type ratio, aminoacylation of tRNACys is not detectable Escherichia coli
E354Q the ratio of turnover number to Km-value of aminoacylation of tRNACys is 10% of the wild-type ratio Escherichia coli
H206S the ratio of turnover number to Km-value of aminoacylation of tRNACys is 60% of the wild-type ratio Escherichia coli
H224N/H235N the ratio of turnover number to Km-value of aminoacylation of tRNACys is 0.042% of the wild-type ratio Escherichia coli
H224S the ratio of turnover number to Km-value of aminoacylation of tRNACys is 5.7% of the wild-type ratio Escherichia coli
H234N/E238Q the ratio of turnover number to Km-value of aminoacylation of tRNACys is 0.0059% of the wild-type ratio Escherichia coli
H234N/E238Q/H224N/H235N aminoacylation of tRNACys is not detectable Escherichia coli
H234S the ratio of turnover number to Km-value of aminoacylation of tRNACys is 0.015% of the wild-type ratio Escherichia coli
H235S the ratio of turnover number to Km-value of aminoacylation of tRNACys is 0.38% of the wild-type ratio Escherichia coli
H238S the ratio of turnover number to Km-value of aminoacylation of tRNACys is 30% of the wild-type ratio Escherichia coli
H256S the ratio of turnover number to Km-value of aminoacylation of tRNACys is 10% of the wild-type ratio Escherichia coli
N351D the ratio of turnover number to Km-value of aminoacylation of tRNACys is 0.25% of the wild-type ratio Escherichia coli
W205F the ratio of turnover number to Km-value of aminoacylation of tRNACys is 0.55% of the wild-type ratio Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.00116
-
 tRNACys 37°C, wild-type enzyme Escherichia coli
0.25
-
 ATP pH 8.0, wild-type enzyme, ATP-diphosphate exchange Escherichia coli
0.31
-
 ATP pH 8.0, mutant enzyme DELTA288-461, ATP-diphosphate exchange Escherichia coli
1.18
-
 ATP pH 8.0, mutant enzyme DELTA328-461, ATP-diphosphate exchange Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + L-cysteine + tRNACys
-
 Escherichia coli AMP + diphosphate + L-cysteinyl-tRNACys
-
 ?

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.34
-
 ATP pH 8.0, mutant enzyme DELTA328-461, ATP-diphosphate exchange Escherichia coli
2
-
 ATP pH 8.0, mutant enzyme DELTA288-461, ATP-diphosphate exchange Escherichia coli
2.46
-
 tRNACys 37°C, wild-type enzyme Escherichia coli
22.6
-
 ATP pH 8.0, wild-type enzyme, ATP-diphosphate exchange Escherichia coli