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Substrate recognition by "password" in p-hydroxybenzoate hydroxylase.
Biochemistry. 1999 Jan 26; 38(4):1153-8.B

Abstract

The flavin of p-hydroxybenzoate hydroxylase (PHBH) adopts two conformations [Gatti, D. L., Palfey, B. A., Lah, M.-S., Entsch, B., Massey, V., Ballou, D. P., and Ludwig, M. L. (1994) Science 266, 110-114; Schreuder, H. A., Mattevi, A., Obmolova, G., Kalk, K. H., Hol, W. G. J., van der Bolt, F. J. T., and van Berkel, W. J. H. (1994) Biochemistry 33, 10161-10170]. Kinetic studies detected the movement of the flavin from the buried conformation to the exposed conformation caused by the binding of NADPH prior to its reaction with the flavin. The pH dependence of the rate constant for flavin reduction in wild-type PHBH and the His72Asn mutant indicates that the deprotonation of bound p-hydroxybenzoate is also required for flavin movement, and is accomplished by the same internal proton transport network previously found to be involved in substrate oxidation. The linkage of substrate deprotonation to flavin movement constitutes a novel mode of molecular recognition in which the enzyme tests the suitability of aromatic substrates before committing to the catalytic cycle.

Authors+Show Affiliations

Department of Biological Chemistry, University of Michigan, Ann Arbor, Michigan 48109-0606, USA. brupalf@umich.eduNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, P.H.S.

Language

eng

PubMed ID

9930974

Citation

Palfey, B A., et al. "Substrate Recognition By "password" in P-hydroxybenzoate Hydroxylase." Biochemistry, vol. 38, no. 4, 1999, pp. 1153-8.
Palfey BA, Moran GR, Entsch B, et al. Substrate recognition by "password" in p-hydroxybenzoate hydroxylase. Biochemistry. 1999;38(4):1153-8.
Palfey, B. A., Moran, G. R., Entsch, B., Ballou, D. P., & Massey, V. (1999). Substrate recognition by "password" in p-hydroxybenzoate hydroxylase. Biochemistry, 38(4), 1153-8.
Palfey BA, et al. Substrate Recognition By "password" in P-hydroxybenzoate Hydroxylase. Biochemistry. 1999 Jan 26;38(4):1153-8. PubMed PMID: 9930974.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Substrate recognition by "password" in p-hydroxybenzoate hydroxylase. AU - Palfey,B A, AU - Moran,G R, AU - Entsch,B, AU - Ballou,D P, AU - Massey,V, PY - 1999/2/4/pubmed PY - 1999/2/4/medline PY - 1999/2/4/entrez SP - 1153 EP - 8 JF - Biochemistry JO - Biochemistry VL - 38 IS - 4 N2 - The flavin of p-hydroxybenzoate hydroxylase (PHBH) adopts two conformations [Gatti, D. L., Palfey, B. A., Lah, M.-S., Entsch, B., Massey, V., Ballou, D. P., and Ludwig, M. L. (1994) Science 266, 110-114; Schreuder, H. A., Mattevi, A., Obmolova, G., Kalk, K. H., Hol, W. G. J., van der Bolt, F. J. T., and van Berkel, W. J. H. (1994) Biochemistry 33, 10161-10170]. Kinetic studies detected the movement of the flavin from the buried conformation to the exposed conformation caused by the binding of NADPH prior to its reaction with the flavin. The pH dependence of the rate constant for flavin reduction in wild-type PHBH and the His72Asn mutant indicates that the deprotonation of bound p-hydroxybenzoate is also required for flavin movement, and is accomplished by the same internal proton transport network previously found to be involved in substrate oxidation. The linkage of substrate deprotonation to flavin movement constitutes a novel mode of molecular recognition in which the enzyme tests the suitability of aromatic substrates before committing to the catalytic cycle. SN - 0006-2960 UR - https://www.unboundmedicine.com/medline/citation/9930974/Substrate_recognition_by_"password"_in_p_hydroxybenzoate_hydroxylase_ L2 - https://doi.org/10.1021/bi9826613 DB - PRIME DP - Unbound Medicine ER -