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Binding of coenzyme and substrate and coenzyme analogues to 6-phosphogluconate dehydrogenase from sheep liver. An X-ray study at 0.6 nm resolution.
Eur J Biochem. 1979 Jul; 98(1):121-30.EJ

Abstract

The analogues of the coenzyme NADP+, nicotinamide--8-bromo-adenine dinucleotide phosphate (Nbr8ADP+) and 3-iodopyridine--adenine dinucleotide phosphate (io3PdADP+), were prepared. Nbr8ADP+ was found to be active in the hydrogen transfer adn io3PdADP+ is a coenzyme competitive inhibitor for 6-phosphogluconate dehydrogenase. The binding of NADP+, NADPH and NADPH together with 6-phosphogluconate as well as that of both analogues to crystals of the enzyme 6-phosphogluconate dehydrogenase has been investigated at 0.6-nm resolution using difference electron density maps. The molecules bind in a similar position in a cleft in the enzyme subunit distant from the dimer interface. The orientation of the coenzyme in the site has been determined from the io3PdADP+ -NADP+ difference density. The ternary complex difference density extends beyond that of the nicotinamide moiety of the coenzyme and tentatively indicates substrate binding. No clear identification of the bromine atom of Nbr8ADP+ can be made. However, the analogue is bound more deeply in the cleft than is NADP+. The NADPH density is the most clearly defined and has thus been used to fit a molecular model using an interactive graphics system, checking for preferred geometry. A possible conformation is presented which is significantly different from that of NAD+ in the lactate dehydrogenase ternary complex.

Authors

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Pub Type(s)

Journal Article

Language

eng

PubMed ID

38116

Citation

Abdallah, M A., et al. "Binding of Coenzyme and Substrate and Coenzyme Analogues to 6-phosphogluconate Dehydrogenase From Sheep Liver. an X-ray Study at 0.6 Nm Resolution." European Journal of Biochemistry, vol. 98, no. 1, 1979, pp. 121-30.
Abdallah MA, Adams MJ, Archibald IG, et al. Binding of coenzyme and substrate and coenzyme analogues to 6-phosphogluconate dehydrogenase from sheep liver. An X-ray study at 0.6 nm resolution. Eur J Biochem. 1979;98(1):121-30.
Abdallah, M. A., Adams, M. J., Archibald, I. G., Biellmann, J. F., Helliwell, J. R., & Jenkins, S. E. (1979). Binding of coenzyme and substrate and coenzyme analogues to 6-phosphogluconate dehydrogenase from sheep liver. An X-ray study at 0.6 nm resolution. European Journal of Biochemistry, 98(1), 121-30.
Abdallah MA, et al. Binding of Coenzyme and Substrate and Coenzyme Analogues to 6-phosphogluconate Dehydrogenase From Sheep Liver. an X-ray Study at 0.6 Nm Resolution. Eur J Biochem. 1979;98(1):121-30. PubMed PMID: 38116.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Binding of coenzyme and substrate and coenzyme analogues to 6-phosphogluconate dehydrogenase from sheep liver. An X-ray study at 0.6 nm resolution. AU - Abdallah,M A, AU - Adams,M J, AU - Archibald,I G, AU - Biellmann,J F, AU - Helliwell,J R, AU - Jenkins,S E, PY - 1979/7/1/pubmed PY - 1979/7/1/medline PY - 1979/7/1/entrez SP - 121 EP - 30 JF - European journal of biochemistry JO - Eur. J. Biochem. VL - 98 IS - 1 N2 - The analogues of the coenzyme NADP+, nicotinamide--8-bromo-adenine dinucleotide phosphate (Nbr8ADP+) and 3-iodopyridine--adenine dinucleotide phosphate (io3PdADP+), were prepared. Nbr8ADP+ was found to be active in the hydrogen transfer adn io3PdADP+ is a coenzyme competitive inhibitor for 6-phosphogluconate dehydrogenase. The binding of NADP+, NADPH and NADPH together with 6-phosphogluconate as well as that of both analogues to crystals of the enzyme 6-phosphogluconate dehydrogenase has been investigated at 0.6-nm resolution using difference electron density maps. The molecules bind in a similar position in a cleft in the enzyme subunit distant from the dimer interface. The orientation of the coenzyme in the site has been determined from the io3PdADP+ -NADP+ difference density. The ternary complex difference density extends beyond that of the nicotinamide moiety of the coenzyme and tentatively indicates substrate binding. No clear identification of the bromine atom of Nbr8ADP+ can be made. However, the analogue is bound more deeply in the cleft than is NADP+. The NADPH density is the most clearly defined and has thus been used to fit a molecular model using an interactive graphics system, checking for preferred geometry. A possible conformation is presented which is significantly different from that of NAD+ in the lactate dehydrogenase ternary complex. SN - 0014-2956 UR - https://www.unboundmedicine.com/medline/citation/38116/Binding_of_coenzyme_and_substrate_and_coenzyme_analogues_to_6_phosphogluconate_dehydrogenase_from_sheep_liver__An_X_ray_study_at_0_6_nm_resolution_ L2 - https://onlinelibrary.wiley.com/resolve/openurl?genre=article&sid=nlm:pubmed&issn=0014-2956&date=1979&volume=98&issue=1&spage=121 DB - PRIME DP - Unbound Medicine ER -