Amino acid residues conferring the nucleotide binding properties of N-acetyl-D-glucosamine 2-epimerase (renin binding protein).
Our recent studies have demonstrated that the middle domain of N-acetyl-D-glucosamine (GlcNAc) 2-epimerase participates in the specificity for and binding of nucleotides. To identify the residue conferring nucleotide binding, amino acid substitutions were introduced in the human and rat GlcNAc 2-epimerases. The mutational analyses indicate that residue 171 of GlcNAc 2-epimerase is critical for the nucleotide binding of GlcNAc 2-epimerase.
Takahashi
Saori
S
Department of Bioengineering, Akita Research Institute of Food and Brewing (ARIF), 4-26, Sanuki, Arayamachi, Akita 010-1623, Japan. saori@arif.pref.akita.jp
Ogasawara
Hironobu
H
Hiwatashi
Kazuyuki
K
Hata
Keishi
K
Hori
Kazuyuki
K
Koizumi
Yukio
Y
Sugiyama
Toshihiro
T
D000255:Adenosine Triphosphate / Q000378:metabolism; D000595:Amino Acid Sequence; D000596:Amino Acids / Q000378:metabolism*; D000818:Animals; D002238:Carbohydrate Epimerases / Q000235:genetics / Q000378:metabolism*; D002352:Carrier Proteins / Q000235:genetics / Q000378:metabolism*; D006801:Humans; D008969:Molecular Sequence Data; D009711:Nucleotides / Q000378:metabolism*; D017434:Protein Structure, Tertiary; D051381:Rats
D000596:Amino Acids; D002352:Carrier Proteins; D009711:Nucleotides; D000255:Adenosine Triphosphate; D002238:Carbohydrate Epimerases; C498259:RENBP protein, human