Home LiteratureArticle Details
PMID: 807243 Published · ppublish English Journal Article Research Support, U.S. Gov't, Non-P.H.S.

The effect of substrate analogs on the circular dichroic spectra of thymidylate synthetase from Lactobacillus casei.

Biochemistry ·Vol. 14 ·No. 15 ·1975-07-29 ·Pages 3338-44

Galivan JH, Maley GF, Maley F

Abstract

Circular dichroism studies from 290 to 400 nm with the thymidylate synthetase from Lactobacillus casei revealed characteristic Cotton effects in the presence of various folate analogs plus 5-fluoro-2'-deoxyuridylate. Omission of either substrate analog prevented the appearance of the Cotton effects. When 5-fluoro-2'-deoxyuridylate and (+/-)-5,10-methylenetetrahydrofolate are mixed with the synthetase, a ternary complex results which yields distinctive minor negative ellipicity bands at 285 and 332 nm and a major negative ellipticity bands at 285 and 332 nm and a major positive band at 305 nm. Similar results were obtained with the ternary complex containing (+)-5,10-methylenetetrahydrofolate, but the enzymically inactive (-) diastereoisomer induced only the positive band at 305 nm. More intense Cotton effects were elicited by (+/-)-5,11-methylenetetrahydrohomofolate with a major positive ellipticity band at 308 nm and a minor negative band at 335 nm. A ternary complex was also formed with dihydrofolate, which provided a major circular dichroic band at 305 nm and a broad minor negative band in the region of 335 nm. Deoxyuridylate and thymidylate also formed ternary complexes with dihydrofolate, but their ellipicity bands were much less intense. Other folate analogs that formed ternary complexes with 5-fluoro-2'-deoxyuridylate to provide characteristic circular dichroic spectra were tetrahydrofolate, tetrahydrohomofolate, 10-methyltetrahydrofolate, and a 2-amino-4-hydroxyquinazoline derivative. By measuring the increment in ellipticity at 305 nm on addition of specific ligands to enzyme solutions, it was determined that the L. casei thymidylate synthetase contains two binding sites for 5-fluoro-2'-deoxyuridylate and for each of the diastereoisomers of 5,10-methylenetetrahydrofolate. An improved procedure is presented for the large-scale purification and crystallization of L. casei thymidylate synthetase.

MeSH Terms
Binding Sites Circular Dichroism Fluorodeoxyuridylate/pharmacology Folic Acid Antagonists/pharmacology Kinetics Lactobacillus casei/enzymology Methyltransferases Protein Binding Protein Conformation Spectrophotometry, Ultraviolet Stereoisomerism Structure-Activity Relationship Thymidylate Synthase/metabolism Thymine Nucleotides
Chemicals
Folic Acid Antagonists Thymine Nucleotides Fluorodeoxyuridylate Methyltransferases Thymidylate Synthase
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Galivan J H
Maley G F
Maley F
Article Info
Journal
Biochemistry
Abbr.
Biochemistry
ISSN
0006-2960
Published
1975-07-29
Pages
3338-44
Language
English
Region
United States
NLM ID
0370623
Subset
IM
Analysis Services
Analysis Services

Contact

No. 2 Wenbo Road, Zhangqiu District, Jinan, Shandong

Qilu Normal University · Genelibs Bioinformatics Lab

750 Shunhua Rd, Jinan

2F, Bldg F, University Science Park

Tel: 0531-88819269

WeChat Official Account

Follow our WeChat subscription account for real-time updates and the latest in medical and biological research.


Business Email

E-mail: [email protected]