Ionization of zwitterionic amine substrates bound to monomeric sarcosine oxidase

Biochemistry

Volumn 44, Issue 51, 2005, Pages 16866-16874

  Zhao, Gouhua ^a   Jorns, Marilyn Schuman ^a  

^a DREXEL UNIVERSITY COLLEGE OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CHARGE TRANSFER; ENZYME KINETICS; ENZYMES; IONIZATION; MUTAGENESIS; OXIDATION; PH EFFECTS; TITRATION;

L-PROLINE; MONOMERIC SARCOSINE OXIDASE (MSOX); PROTON TRANSFER;

AMINES;

AMINE; AMINO ACID; AMPHOLYTE; MONOMERIC SARCOSINE OXIDASE; MUTANT PROTEIN; PHENYLALANINE; PROLINE; SARCOSINE OXIDASE; TYROSINE; UNCLASSIFIED DRUG;

AMINO ACID SUBSTITUTION; ARTICLE; CHEMICAL REACTION KINETICS; COMPLEX FORMATION; CONTROLLED STUDY; ENERGY; ENZYME ACTIVE SITE; ENZYME BINDING; IONIZATION; MUTATION; NONHUMAN; OXIDATION; PH; PKA; PRIORITY JOURNAL; PROTON TRANSPORT; REDUCTION;

ACETATES; ALGORITHMS; AMINES; AMINO ACID SUBSTITUTION; ANIONS; BACILLUS; BINDING SITES; CATALYSIS; ENZYME INHIBITORS; HYDROGEN-ION CONCENTRATION; KINETICS; MODELS, CHEMICAL; MODELS, MOLECULAR; MUTATION; OXIDATION-REDUCTION; PROLINE; PROTONS; RECOMBINANT PROTEINS; SARCOSINE; SARCOSINE OXIDASE; SPECTROPHOTOMETRY; SUBSTRATE SPECIFICITY; TITRIMETRY; TYROSINE;

EID: 29344450649     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi051898d     Document Type: Article

References (20)

1. Wagner, M. A., Khanna, P., and Jorns, M. S. (1999) Structure of the flavocoenzyme of two homologous amine oxidases: Monomeric sarcosine oxidase and N-methyltryptophan oxidase, Biochemistry 38, 5588-5595.
2. Trickey, P., Wagner, M. A., Jorns, M. S., and Mathews, F. S. (1999) Monomeric sarcosine oxidase: Structure of a covalently-flavinylated secondary amine oxidizing enzyme, Structure 7, 331-345.
3. Zhao, G., Song, H., Chen, Z., Mathews, F. S., and Jorns, M. S. (2002) Monomeric sarcosine oxidase: Role of histidine 269 in catalysis, Biochemistry 41, 9751-9764.
4. Wagner, M. A., Trickey, P., Chen, Z., Mathews, F. S., and Jorns, M. S. (2000) Monomeric sarcosine oxidase: 1. Flavin reactivity and active site binding determinants. Biochemistry 39, 8813-8824.
5. Khanna, P., and Jorns, M. S. (2001) Characterization of the FAD-containing N-methyltryptophan oxidase from Escherichia coli, Biochemistry 40, 1441-1450.
6. Venci, D., Zhao, G., and Jorns, M. S. (2002) Molecular characterization of nikD, a new flavoenzyme important in the biosynthesis of nikkomycin antibiotics. Biochemistry 41, 15795-15802.
7. Eschenbrenner, M., Chlumsky, L. J., Khanna, P., Strasser, F., and Jorns, M. S. (2001) Organization of the multiple coenzymes and subunits and role of the covalent flavin link in the complex heterotetrameric sarcosine oxidase, Biochemistry 40, 5352-5367.
8. Dodt, G., Kim, D. G., Reimann, S. A., Reuber, B. E., McCabe, K., Gould, S. J., and Mihalik, S. J. (2000) L-pipecolic acid oxidase, a human enzyme essential for the degradation of L-pipecolic acid, is most similar to the monomeric sarcosine oxidases, Biochem. J. 345, 487-494.
9. Silverman, R. B. (1995) Radical ideas about monoamine oxidase, Acc. Chem. Res. 28, 335-342.
10. Kim, J. M., Hoegy, S. E., and Mariano, P. S. (1995) Flavin chemical models for monoamine oxidase inactivation by cyclopropylamines, alpha-silylamines, and hydrazines, J. Am. Chem. Soc. 117, 100-105.
11. Silverman, R. B., and Zelechonok, Y. (1992) Evidence for a hydrogen atom transfer mechanism or a proton fast electron-transfer mechanism for monoamine oxidase, J. Org. Chem. 57, 6373-6374.
12. Miller, J. R., and Edmondson, D. E. (1999) Structure-activity relationships in the oxidation of para-substituted benzylamine analogues by recombinant human liver monoamine oxidase A, Biochemistry 38, 13670-13683.
13. Harris, C. M., Pollegioni, L., and Ghisla, S. (2001) pH and kinetic isotope effects in D-amino acid oxidase catalysis-Evidence for a concerted mechanism in substrate dehydrogenation via hydride transfer, Eur. J. Biochem. 268, 5504-5520.
14. Zhao, G. H., and Jorns, M. S. (2002) Monomeric sarcosine oxidase: Evidence for an ionizable group in the ES complex, Biochemistry 41, 9747-9750.
15. Ho, S. N., Hunt, H. D., Horton, R. M., Pullen, J. K., and Pease, L. R. (1989) Site-directed mutagenesis by overlap extension using the polymerase chain reaction, Gene 77, 51-59.
16. Wagner, M. A., and Jorns, M. S. (2000) Monomeric sarcosine oxidase: 2. Kinetic studies with sarcosine, alternate substrates and substrate analogs, Biochemistry 39, 8825-8829.
17. Strickland, S., Palmer, G., and Massey, V. (1975) Determination of dissociation constants and specific rate constants of enzyme-substrate (or protein-ligand) interactions from rapid reaction kinetic data, J. Biol. Chem. 250, 4048-4052.
18. Basran, J., Sutcliffe, M. J., and Scrutton, N. S. (2001) Optimizing the Michaelis complex of trimethylamine dehydrogenase-Identification of interactions that perturb the ionization of substrate and facilitate catalysis with trimethylamine base, J. Biol. Chem. 276, 42887-42892.
19. Shieh, H.-S., Ghisla, S., Hanson, L. K., Ludwig, M. L., and Nordman, C. E. (1981) Molecular complex of lumiflavin and 2-aminobenzoic acid: Crystal structure, crystal spectra and solutions properties, Biochemistry 20, 4766-4774.
20. Dmitrenko, O., Thorpe, C., and Bach, R. D. (2003) Effect of a charge-transfer interaction on the catalytic activity of acyl-CoA dehydrogenase: A theoretical study of the role of oxidized flavin, J. Phys. Chem. B 107, 13229-13236.