Abstract:
:The amino acid residue Asn141 of the restriction endonuclease EcoRI was proposed to make three hydrogen bonds to both adenine residues within the recognition sequence -GAATTC-. We have mutated Asn141 to alanine, aspartate, serine, and tyrosine. Only the serine mutant is active under normal buffer conditions although 1000-fold less than wild-type EcoRI. The alanine and aspartate mutants can be activated by Mn2+. At acidic pH the latter mutant becomes even more active than the wild-type enzyme in the presence of Mn2+. We conclude that Asn141 is essential for DNA recognition and that serine can partly substitute it.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Fritz A,Küster W,Alves Jdoi
10.1016/s0014-5793(98)01274-5subject
Has Abstractpub_date
1998-10-30 00:00:00pages
66-70issue
1-2eissn
0014-5793issn
1873-3468pii
S0014-5793(98)01274-5journal_volume
438pub_type
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