SPECIFICITY OF GUANYLIC RNASES TO POLYNUCLEOTIDE SUBSTRATES

被引：9

作者：

BOTH, V ^{[1
]}

MOISEYEV, GP ^{[1
]}

SEVCIK, J ^{[1
]}

机构：

[1] VA ENGELHARDT MOLEC BIOL INST, MOSCOW, USSR

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1991年 / 177卷 / 02期

关键词：

D O I：

10.1016/0006-291X(91)91835-Z

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Kinetic parameters kcat and Km were measured for cleavage of poly I, poly A, poly U, poly C and poly I. poly C by guanyl-specific RNases Sa, Pb1 and T1 and compared with that of guanyl-preferential RNase Bi. Catalytic efficiencies of the investigated enzymes to polynucleotide substrates vary considerably. The structural basis for specificity of these RNases is discussed. A hypothesis is suggested that Ser-56 plays an important role in recognition of poly A by RNase Bi. © 1991.

引用

页码：630 / 635

页数：6

共 21 条

[1]

BEZBORODOVA S I, 1974, Prikladnaya Biokhimiya i Mikrobiologiya, V10, P432

[2] POLYNUCLEOTIDES .7. SPECTROPHOTOMETRIC STUDY OF KINETICS OF FORMATION OF 2-STRANDED HELICAL COMPLEX RESULTING FROM INTERACTION OF POLYRIBOADENYLATE AND POLYRIBOURIDYLATE [J].