The charge state of substrates and inhibitors when bound to Lactobacillus casei dihydrofolate reductase [proceedings]
- PMID: 20381
- DOI: 10.1042/bst0050771
The charge state of substrates and inhibitors when bound to Lactobacillus casei dihydrofolate reductase [proceedings]
Similar articles
-
Ultraviolet difference-spectroscopic studies of substrate and inhibitor binding to Lactobacillus casei dihydrofolate reductase.Biochem J. 1978 May 1;171(2):357-66. doi: 10.1042/bj1710357. Biochem J. 1978. PMID: 26334 Free PMC article.
-
Reduction of oxidised folates by dihydrofolate reductase from methotrexate-resistant Lactobacillus casei.Biochim Biophys Acta. 1977 Jun 10;482(2):261-71. doi: 10.1016/0005-2744(77)90240-6. Biochim Biophys Acta. 1977. PMID: 18181
-
Dihydrofolate reductase from amethopterin-resistant Lactobacillus casei. Effects of pH, salts, temperature, and source of NADPH on enzyme activity and substrate specificity studies.Arch Biochem Biophys. 1977 Jun;181(2):569-79. doi: 10.1016/0003-9861(77)90263-6. Arch Biochem Biophys. 1977. PMID: 20050 No abstract available.
-
Dihydrofolate reductase: binding of substrates and inhibitors and catalytic mechanism.Adv Pharmacol Chemother. 1980;17:37-102. doi: 10.1016/s1054-3589(08)60007-1. Adv Pharmacol Chemother. 1980. PMID: 7004143 Review. No abstract available.
-
Dihydrofolate reductases: structural and mechanistic aspects.Ann N Y Acad Sci. 1971 Nov 30;186:85-99. Ann N Y Acad Sci. 1971. PMID: 4400072 Review. No abstract available.
Cited by
-
Ultraviolet difference-spectroscopic studies of substrate and inhibitor binding to Lactobacillus casei dihydrofolate reductase.Biochem J. 1978 May 1;171(2):357-66. doi: 10.1042/bj1710357. Biochem J. 1978. PMID: 26334 Free PMC article.
MeSH terms
Substances
LinkOut - more resources
Full Text Sources