Arginine residues involved in binding of tetrahydrofolate to sheep liver serine hydroxymethyltransferase.
Open Access
- 1 May 1992
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 267 (13) , 9289-9293
- https://doi.org/10.1016/s0021-9258(19)50421-5
Abstract
No abstract availableKeywords
This publication has 20 references indexed in Scilit:
- Conversion of arginine to lysine at position 70 of human dihydrofolate reductase: generation of a methotrexate-insensitive mutant enzymeBiochemistry, 1991
- Mode of interaction of aminooxy compounds with sheep liver serine hydroxymethyltransferaseBiochemistry, 1989
- Mechanism of interaction of O-amino-D-serine with sheep liver serine hydroxymethyltransferaseBiochemistry, 1989
- Identification of active-site residues of sheep liver serine hydroxymethyltransferaseBiochemical Journal, 1984
- Enzymes of serine metabolism in normal, developing and neoplastic rat tissuesAdvances in Enzyme Regulation, 1984
- Complete nucleotide sequence of theE. coli glyAgeneNucleic Acids Research, 1983
- Studies on identifying the folylpolyglutamate binding sites of Lactobacillus casei thymidylate synthetaseArchives of Biochemistry and Biophysics, 1982
- Micro‐sequence analysis of peptides and proteins using 4‐NN‐dimethylaminoazobenzene 4′‐isothiocyanate/phenylisothiocyanate double coupling methodFEBS Letters, 1978
- The mechanism of action of serine transhydroxymethylaseBiochemical Journal, 1970
- [19] Performic acid oxidationPublished by Elsevier ,1967