Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)

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Gene Review:

hisS - histidine--tRNA ligase

Salmonella enterica subsp. enterica serovar Typhimurium str. LT2

Lepore, G.C. et al., Di Natale, P. et al., Lepore, G.C. et al.

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Disease relevance of hisS

Structural requirements for substrate binding to histidyl-tRNA synthetase from Salmonella typhimurium have been investigated using ATP analogues [1].

High impact information on hisS

The interaction of histidyl-tRNA synthetase, a dimeric enzyme, with histidine and ATP was examined by fluorescence measurements at equilibrium and by equilibrium dialysis [1].
The reactivity of the sulfhydryl groups of histidyl-t RNA synthetase from Salmonella typhimurium and the effect of substrates on the reactivity has been studied using p-hydroxymercuribenzoate and 5, 5'-dithiobis (2-nitrobenzoic acid) as reagents [2].
The topography of the active site of histidyl-tRNA synthetase has been investigated by determining Ki values for a variety of structural analogues of histidine, using the ATP-PPi exchange and tRNA aminoacylation reactions [3].

Chemical compound and disease context of hisS

Histidyl-tRNA synthetase from Salmonella typhimurium: specificity in the binding of histidine analogues [3].

References

Histidyl transfer ribonucleic acid synthetase from Salmonella typhimurium. Interaction with substrates and ATP analogues. Di Natale, P., Schechter, A.N., Castronuovo Lepore, G., De Lorenzo, F. Eur. J. Biochem. (1976) [Pubmed]
Histidyl-transfer-ribonucleic-acid synthetase from Salmonella typhimurium. Studies of the sulfhydryl groups. Lepore, G.C., Geraci, G., Abrescia, P., de Lorenzo, F. Eur. J. Biochem. (1976) [Pubmed]
Histidyl-tRNA synthetase from Salmonella typhimurium: specificity in the binding of histidine analogues. Lepore, G.C., Di Natale, P., Guarini, L., De Lorenzo, F. Eur. J. Biochem. (1975) [Pubmed]

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