TY - JOUR
T1 - Yeast pyruvate kinase
T2 - essential lysine residues in the active site
AU - Imarai, Mónica
AU - Hinrichsen, Patricio
AU - Bazaes, Sergio
AU - Wilkens, Marcela
AU - Eyzaguirre, Jaime
PY - 1988/1/1
Y1 - 1988/1/1
N2 - 1. 1. Yeast pyruvate kinase was purified to near homogeneity and subjected to chemical modification by trinitrobenzenesulfbnate and by P1, P2-bis (5′ pyridoxal) diphosphate. 2. 2. Labeled peptides were isolated and their amino acid composition was determined. 3. 3. The results suggest that yeast pyruvate kinase has an essential lysine residue, and that this residue is in a location equivalent to an essential lysine described in the muscle enzyme. 4. 4. Protection experiments indicate that this lysine is located at the nucleotide binding site.
AB - 1. 1. Yeast pyruvate kinase was purified to near homogeneity and subjected to chemical modification by trinitrobenzenesulfbnate and by P1, P2-bis (5′ pyridoxal) diphosphate. 2. 2. Labeled peptides were isolated and their amino acid composition was determined. 3. 3. The results suggest that yeast pyruvate kinase has an essential lysine residue, and that this residue is in a location equivalent to an essential lysine described in the muscle enzyme. 4. 4. Protection experiments indicate that this lysine is located at the nucleotide binding site.
UR - http://www.scopus.com/inward/record.url?scp=0024254461&partnerID=8YFLogxK
U2 - 10.1016/0020-711X(88)90188-7
DO - 10.1016/0020-711X(88)90188-7
M3 - Article
C2 - 3143610
AN - SCOPUS:0024254461
VL - 20
SP - 1001
EP - 1008
JO - International Journal of Biochemistry
JF - International Journal of Biochemistry
SN - 1357-2725
IS - 9
ER -