TY - JOUR
T1 - Specificities of acetoxy derivatives of coumarins, biscoumarins, chromones, flavones, isoflavones and xanthones for acetoxy drug
T2 - Protein transacetylase
AU - Kumar, Ajit
AU - Singh, Brajendra K.
AU - Sharma, Nawal K.
AU - Gyanda, Kapil
AU - Jain, Sapan K.
AU - Tyagi, Yogesh K.
AU - Baghel, Anil S.
AU - Pandey, Mukesh
AU - Sharma, Sunil K.
AU - Prasad, Ashok K.
AU - Jain, Subhash C.
AU - Rastogi, Ramesh C.
AU - Raj, Hanumantharao G.
AU - Watterson, Arthur C.
AU - Van der Eycken, Erik
AU - Parmar, Virinder S.
N1 - Funding Information:
This work was supported by Department of Biotechnology (DBT), Department of Science & Technology (DST) and Council of Scientific and Industrial Research (CSIR), Government of India. A.K. and S.K.J. are fellows of CSIR.
PY - 2007/4
Y1 - 2007/4
N2 - The earlier work carried out in our laboratory led to the identification of a novel rat liver microsomal enzyme termed as acetoxy drug: protein transacetylase (TAase), catalyzing the transfer of acetyl group from polyphenolic acetates (PA) to functional proteins. In this paper, we have reported the comparison of the specificities of acetoxy derivatives of coumarins, biscoumarins, chromones, flavones, isoflavones and xanthones with special reference to the phenyl moiety/bulky group on the pyran ring of PA. The results clearly indicated that compounds having phenyl moieties, when used as the substrates, resulted in a significant reduction of TAase catalyzed activity. The alteration in TAase catalyzed activation of NADPH cytochrome c reductase and inhibition of benzene-induced micronuclei in bone marrow cells by PA were in tune with their specificities to TAase.
AB - The earlier work carried out in our laboratory led to the identification of a novel rat liver microsomal enzyme termed as acetoxy drug: protein transacetylase (TAase), catalyzing the transfer of acetyl group from polyphenolic acetates (PA) to functional proteins. In this paper, we have reported the comparison of the specificities of acetoxy derivatives of coumarins, biscoumarins, chromones, flavones, isoflavones and xanthones with special reference to the phenyl moiety/bulky group on the pyran ring of PA. The results clearly indicated that compounds having phenyl moieties, when used as the substrates, resulted in a significant reduction of TAase catalyzed activity. The alteration in TAase catalyzed activation of NADPH cytochrome c reductase and inhibition of benzene-induced micronuclei in bone marrow cells by PA were in tune with their specificities to TAase.
KW - Glutathione S-transferase (GST)
KW - Micronuclei modulation
KW - NADPH cytochrome c reductase
KW - Polyphenolic acetates
KW - Protein transacetylase (TAase)
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U2 - 10.1016/j.ejmech.2006.09.008
DO - 10.1016/j.ejmech.2006.09.008
M3 - Article
C2 - 17182154
AN - SCOPUS:34047187418
SN - 0223-5234
VL - 42
SP - 447
EP - 455
JO - European Journal of Medicinal Chemistry
JF - European Journal of Medicinal Chemistry
IS - 4
ER -