Mutational analysis of the putative substrate-binding site of 3C proteinase of coxsackievirus B3.
Single amino acid substitutions were introduced into the putative substrate-binding site of 3C proteinase (3Cpro) of coxsackievirus B3, a member of the picornavirus family. Mutations at either Thr142, His161, Gly164, Gly169, or Ala172 severely impaired or abolished the proteolytic activity except that a conservative Thr142 to Ser mutant had detectable activity. These results, which have shown the participation of the 5 residues in 3Cpro activity, are consistent with the earlier predictions that these residues might be involved in substrate binding.
Miyashita
K
K
Central Research Laboratories, Maruishi Pharmaceutical Co., Ltd., Osaka, Japan.
Utsumi
R
R
Utsumi
T
T
Komano
T
T
Satoh
N
N
D000409:Alanine / Q000737:chemistry / Q000235:genetics; D000595:Amino Acid Sequence; D001483:Base Sequence; D001665:Binding Sites; D017124:Conserved Sequence; D017931:DNA Primers / Q000737:chemistry; D004591:Electrophoresis, Polyacrylamide Gel; D010450:Endopeptidases / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism; D029822:Enterovirus B, Human / Q000201:enzymology* / Q000235:genetics; D004926:Escherichia coli / Q000201:enzymology / Q000235:genetics; D005998:Glycine / Q000737:chemistry / Q000235:genetics; D006639:Histidine / Q000737:chemistry / Q000235:genetics; D008969:Molecular Sequence Data; D009154:Mutation / Q000235:genetics*; D016415:Sequence Alignment; D012694:Serine / Q000737:chemistry / Q000235:genetics; D013912:Threonine / Q000737:chemistry / Q000235:genetics
D017931:DNA Primers; D013912:Threonine; D012694:Serine; D006639:Histidine; D010450:Endopeptidases; D000409:Alanine; D005998:Glycine