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PMID: 3027698 Published · ppublish English Journal Article

Amino acid sequence of S-adenosyl-L-homocysteine hydrolase from rat liver as derived from the cDNA sequence.

Ogawa H, Gomi T, Mueckler MM, Fujioka M, Backlund PS, Aksamit RR, Unson CG, Cantoni GL

Abstract

Rat liver cDNA libraries constructed in lambda gt11 were screened for reactivity with polyclonal antibodies to native S-adenosyl-L-homocysteine (AdoHcy) hydrolase (adenosylhomocysteinase; EC 3.3.1.1). Five clones were isolated and sequenced. The amino acid sequence, deduced from the cDNA sequence, contained the sequence of eight peptides obtained by tryptic and cyanogen bromide fragmentation of rat liver AdoHcy hydrolase. Identification of the amino- and carboxyl-terminal peptides in the amino acid sequence showed that the complete sequence was obtained. A "fingerprint" sequence was found that is characteristic of dinucleotide-binding domains of many proteins. For AdoHcy hydrolase, this region from the lysine at position 213 to the aspartate at position 244, containing the sequence Gly-Xaa-Gly-Xaa-Xaa-Gly at positions 219-224, is presumably the site of binding for NAD+, which is required for the activity of the enzyme.

MeSH Terms
Adenosylhomocysteinase Amino Acid Sequence Animals Base Sequence Cloning, Molecular DNA/analysis DNA Restriction Enzymes Hydrolases/genetics Liver/enzymology Peptide Fragments/analysis Rats Sequence Homology, Nucleic Acid
Chemicals
Peptide Fragments DNA Hydrolases DNA Restriction Enzymes Adenosylhomocysteinase
Authors & Affiliations
8 authors, click to expand affiliations / ORCID
Ogawa H
Gomi T
Mueckler M M
Fujioka M
Backlund P S
Aksamit R R
Unson C G
Cantoni G L
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
Published
1987-02-00
Pages
719-23
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC304287
Subset
IM
Databases
GENBANK
M15185
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