Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
malfunction
-
impairment of zygotic Sars function leads to a significant dilatation of the aortic arch vessels and aberrant branching of cranial and intersegmental vessels
evolution
-
although SerRSs from methanogenic archaea recognize tRNAsSer from all three domains of life in vitro, the toxicity presumably precludes the complementation of endogenous SerRS function in both, Escherichia coli and Saccharomyces cerevisiae
evolution
-
although SerRSs from methanogenic archaea recognize tRNAsSer from all three domains of life in vitro, the toxicity presumably precludes the complementation of endogenous SerRS function in both, Escherichia coli and Saccharomyces cerevisiae
evolution
-
as a consequence of an N-terminal insertion and a C-terminal extra-sequence, the binding mode of tRNASer to hsSerRS differs from that in prokaryotes
evolution
SerRS belongs to the class II aminoacyl-tRNA synthetases (aaRSs), evolutionary analysis of SerRS and TyrRS, overview
evolution
the enzyme belongs to the class II, subclass IIa, of aminoacyl-tRNA sythetases
evolution
-
the enzyme belongs to the class II, subclass IIa, of aminoacyl-tRNA sythetases
-
evolution
-
the enzyme belongs to the class II, subclass IIa, of aminoacyl-tRNA sythetases
-
physiological function
seryl-tRNA synthetase is involved in vascular development
physiological function
-
seryl-tRNA synthetase possesses an angiogenesis-regulating capacity
physiological function
-
seryl-tRNA synthetase possesses an angiogenesis-regulating capacity
physiological function
seryl-tRNA synthetase is an essential enzyme for translation, also regulating vascular development
physiological function
aminoacyl-tRNA synthetases (aaRSs) for glycine, alanine, serine and tyrosine play important roles in fibroin synthesis
additional information
-
expression of methanogenic-type SerRSs is toxic for Escherichia coli cells
additional information
-
expression of methanogenic-type SerRSs is toxic for Escherichia coli cells
additional information
the interactions between the catalytically important loops and tRNA contribute to the change in dynamics of tRNA in free and bound states, respectively. These interactions help in the development of catalytically effective organization of the active site. The A76 end of the tttRNASer exhibits fast dynamics in free state, which is significantly reduced within the active site bound with adenylate. Presence of bound Mg2+ ions around tRNA and dynamically slow bound water are other common features of the enzyme, dynamics of dimeric ttSerRS bound with adenylate and tttRNASer with a focus to the molecular process of the dynamic development of the catalytically competent active site organization essential for the second step, molecular dynamic simulations, overview
additional information
-
the interactions between the catalytically important loops and tRNA contribute to the change in dynamics of tRNA in free and bound states, respectively. These interactions help in the development of catalytically effective organization of the active site. The A76 end of the tttRNASer exhibits fast dynamics in free state, which is significantly reduced within the active site bound with adenylate. Presence of bound Mg2+ ions around tRNA and dynamically slow bound water are other common features of the enzyme, dynamics of dimeric ttSerRS bound with adenylate and tttRNASer with a focus to the molecular process of the dynamic development of the catalytically competent active site organization essential for the second step, molecular dynamic simulations, overview
additional information
-
the interactions between the catalytically important loops and tRNA contribute to the change in dynamics of tRNA in free and bound states, respectively. These interactions help in the development of catalytically effective organization of the active site. The A76 end of the tttRNASer exhibits fast dynamics in free state, which is significantly reduced within the active site bound with adenylate. Presence of bound Mg2+ ions around tRNA and dynamically slow bound water are other common features of the enzyme, dynamics of dimeric ttSerRS bound with adenylate and tttRNASer with a focus to the molecular process of the dynamic development of the catalytically competent active site organization essential for the second step, molecular dynamic simulations, overview
-
additional information
-
the interactions between the catalytically important loops and tRNA contribute to the change in dynamics of tRNA in free and bound states, respectively. These interactions help in the development of catalytically effective organization of the active site. The A76 end of the tttRNASer exhibits fast dynamics in free state, which is significantly reduced within the active site bound with adenylate. Presence of bound Mg2+ ions around tRNA and dynamically slow bound water are other common features of the enzyme, dynamics of dimeric ttSerRS bound with adenylate and tttRNASer with a focus to the molecular process of the dynamic development of the catalytically competent active site organization essential for the second step, molecular dynamic simulations, overview
-