Human extracellular ribonucleases: multiplicity, molecular diversity and catalytic properties of the major RNase types.
Human extracellular ribonucleases (RNase), together with other members of the mammalian RNase A superfamily, can be classified into four different RNase families on the basis of their structural, catalytic and/or biological properties. Their occurrence and main distinctive features have been described, and the information available on their catalytic properties has been analysed and discussed in comparison with those of other animal RNases. On the basis of some results obtained with various single- and double-stranded polyribonucleotides, it has been proposed that while pancreatic-type (pt) RNases could be defined as single-strand/pyrimidine 'preferring' ribonucleases, mammalian nonpancreatic-type (npt) RNases may be referred to as single-strand/pyrimidine 'specific' ribonucleases. In addition, some data concerning human nptRNases may support the suggestion [Cuchillo et al. (1993) FEBS Lett. 333: 207-210] that the enzyme 'ribonuclease' should be reclassified as 'transferase'.
Sorrentino
S
S
Dipartimento di Chimica Organica e Biologica, Università degli Studi di Napoli, Italy.
D000595:Amino Acid Sequence; D000818:Animals; D002384:Catalysis; D005110:Extracellular Space / Q000201:enzymology*; D006801:Humans; D008969:Molecular Sequence Data; D005810:Multigene Family; D012260:Ribonucleases / Q000737:chemistry* / Q000145:classification* / Q000235:genetics / Q000378:metabolism; D017386:Sequence Homology, Amino Acid
D012260:Ribonucleases