The active site of carboxypeptidase Taq possesses the active-site motif His-Glu-X-X-His of zinc-dependent endopeptidases and aminopeptidases.
Carboxypeptidase (CPase) Taq possesses the His-Glu-X-X-His sequence, which is the consensus sequence in the active site of zinc-dependent endopeptidases and amino-peptidases, at positions 276-280. Amino acid replacement of the conserved His and Glu drastically diminished the activity of CPase Taq, and the zinc content of the enzyme was also greatly reduced when either of the two His residues was replaced with Arg or Tyr. The results indicate that this sequence actually functions as the active site in CPase Taq, showing that CPase Taq is a novel type of zinc-dependent CPase that possesses the His-Glu-X-X-His active-site motif.
Lee
S H
SH
Department of Agricultural Chemistry, Japan.
Taguchi
H
H
Yoshimura
E
E
Minagawa
E
E
Kaminogawa
S
S
Ohta
T
T
Matsuzawa
H
H
D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000737:chemistry* / Q000235:genetics; D001483:Base Sequence; D001665:Binding Sites; D002268:Carboxypeptidases / Q000737:chemistry* / Q000235:genetics; D016384:Consensus Sequence; D006639:Histidine / Q000737:chemistry; D016297:Mutagenesis, Site-Directed; D011993:Recombinant Fusion Proteins / Q000737:chemistry; D013824:Thermus / Q000201:enzymology* / Q000235:genetics; D015032:Zinc / Q000032:analysis
D001426:Bacterial Proteins; D011993:Recombinant Fusion Proteins; D006639:Histidine; D002268:Carboxypeptidases; C089478:Thermus aquaticus carboxypeptidase; D015032:Zinc