Title : Histidine residues in human phenol sulfotransferases.

Pub. Date : 2004 Apr 1

PMID : 15013851






4 Functional Relationships(s)
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Compound Name
Protein Name
Organism
1 In this report, the amino acid modification method was used for studies of His residues in the active site of P-PST and M-PST. Histidine sulfotransferase family 1A member 1 Homo sapiens
2 Diethylpyrocarbonate inactivation kinetic data suggest that there is one His residue in the active site that is critical for catalytic activity of both P-PST and M-PST. Histidine sulfotransferase family 1A member 1 Homo sapiens
3 The experimental results agree with amino acid sequence alignment, mutation, and the crystal structures of P-PST and M-PST and suggest that His108 is the only critical His residue in both P-PST and M-PST. Histidine sulfotransferase family 1A member 1 Homo sapiens
4 The experimental results agree with amino acid sequence alignment, mutation, and the crystal structures of P-PST and M-PST and suggest that His108 is the only critical His residue in both P-PST and M-PST. Histidine sulfotransferase family 1A member 1 Homo sapiens