TY - JOUR
T1 - The role of a tyrosyl residue in the mechanism of action of carboxypeptidase B
T2 - luminescence studies
AU - Shaklai, N.
AU - Zisapel, N.
AU - Sokolovsky, M.
PY - 1973
Y1 - 1973
N2 - The luminescence spectra of carboxypeptidase B indicate specific differences between the zinc and apoenzyme due to the state of tyrosyl residues presumably at the active site. These differences disappear when enzyme substrate or enzyme inhibitor complexes are formed, suggesting that they may reflect the interaction of a tyrosyl residue in the native enzyme with the catalytically essential zinc atom. An interpretation of the role of that tyrosyl residue in the mechanism of action of carboxypeptidase B is presented.
AB - The luminescence spectra of carboxypeptidase B indicate specific differences between the zinc and apoenzyme due to the state of tyrosyl residues presumably at the active site. These differences disappear when enzyme substrate or enzyme inhibitor complexes are formed, suggesting that they may reflect the interaction of a tyrosyl residue in the native enzyme with the catalytically essential zinc atom. An interpretation of the role of that tyrosyl residue in the mechanism of action of carboxypeptidase B is presented.
UR - http://www.scopus.com/inward/record.url?scp=0015836907&partnerID=8YFLogxK
U2 - 10.1073/pnas.70.7.2025
DO - 10.1073/pnas.70.7.2025
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AN - SCOPUS:0015836907
SN - 0027-8424
VL - 70
SP - 2025
EP - 2028
JO - Proceedings of the National Academy of Sciences of the United States of America
JF - Proceedings of the National Academy of Sciences of the United States of America
IS - 7
ER -