Enhancement of thermostability of fungal deglycating enzymes by directed evolution

Applied Microbiology and Biotechnology

Volumn 78, Issue 5, 2008, Pages 775-781

  Hirokawa, Kozo ^a   Ichiyanagi, Atsushi ^a   Kajiyama, Naoki ^a  

^a Kikkoman   (Japan)

Author keywords

Directed evolution; Enzymatic measurement of hemoglobin A1c; Fructosyl amino acid oxidase; Fructosyl peptide oxidase; HbA1c

Indexed keywords

ENZYMATIC MEASUREMENT OF HEMOGLOBIN A1C; FRUCTOSYL AMINO ACID OXIDASE; FRUCTOSYL PEPTIDE OXIDASE;

DIAGNOSIS; ENZYME ACTIVITY; MUTAGENESIS; PEPTIDES; THERMODYNAMIC STABILITY;

FUNGI;

AMINO ACID; FRUCTOSYL PEPTIDE OXIDASE; FUNGAL ENZYME; GLYCOPROTEIN; HEMOGLOBIN A1C; MUTANT PROTEIN; OXIDOREDUCTASE; PROTEINASE; UNCLASSIFIED DRUG;

AMINO ACID; DIGESTION; ENZYME ACTIVITY; EVOLUTION; FUNGUS; MUTATION; PIGMENT; PROTEIN;

AMINO ACID SUBSTITUTION; ARTICLE; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME INACTIVATION; ENZYME STABILITY; EVOLUTION; GENE CASSETTE; HALF LIFE TIME; HIGH THROUGHPUT SCREENING; NONHUMAN; SITE DIRECTED MUTAGENESIS; THERMOSTABILITY;

AMINO ACID OXIDOREDUCTASES; AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ASCOMYCOTA; DIRECTED MOLECULAR EVOLUTION; ENZYME STABILITY; FUNGAL PROTEINS; KINETICS; MUTAGENESIS; PROTEIN ENGINEERING; TEMPERATURE;

EID: 41049099149     PISSN: 01757598     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00253-008-1363-z     Document Type: Article

References (24)

1. Bunn HF, Gabbay KH, Gallop PM (1978) The glycosylation of hemoglobin: relevance to diabetes mellitus. Science 200:21-27
2. Consensus Committee (2007) Consensus statement on the worldwide standardization of the hemoglobin A1c measurement: The American Diabetes Association, European Association for the Study of Diabetes, International Federation of Clinical Chemistry and Laboratory Medicine, and the International Diabetes Federation. Diabetologia 50:2042-2043
3. Halwachs-Baumann G, Katzensteiner S, Schnedl W, Pürstner P, Pieber T, Wilders-Truschnig M (1997) Comparative evaluation of three assay systems for automated determination of hemoglobin A1c. Clin Chem 43:511-517
4. Hemsley A, Arnheim N, Toney MD, Cortopassi G, Galas DJ (1989) A simple method for site-directed mutagenesis using the polymerase chain reaction. Nucleic Acids Res 17:6545-6551
5. Hirokawa K, Gomi K, Kajiyama N (2003) Molecular cloning and expression of novel fructosyl peptide oxidases and their application for the measurement of glycated protein. Biochem Biophys Res Commun 311:104-111
6. Hirokawa K, Kajiyama N (2002) Recombinant Agrobacterium AgaE-like protein with fructosyl amino acid oxidase activity. Biosci Biotechnol Biochem 66:2323-2329
7. Hirokawa K, Nakamura K, Kajiyama N (2004) Enzymes used for the determination of HbA1c. FEMS Microbiol Lett 235:157-162
8. Hirokawa K, Shimoji K, Kajiyama N (2005) An enzymatic method for the determination of hemoglobin A1c. Biotechnol Lett 27:963-968
9. Horiuchi T, Kurokawa T, Saito N (1989) Purification and properties of fructosyl-amino acid oxidase from Corynebacterium sp. 2-4-1. Agric Biol Chem 53:103-110
10. Jeong HY, Song MH, Back JH, Han DM, Wu X, Monnier V, Jahng KY, Chae KS (2002) The veA gene is necessary for the inducible expression by fructosyl amines of the Aspergillus nidulans faoA gene encoding fructosyl amino acid oxidase (amadoriase, EC 1.5.3). Arch Microbiol 178:344-350
11. Johannes TW, Woodyer RD, Zhao H (2005) Directed evolution of a thermostable phosphite dehydrogenase for NAD(P)H regeneration. Appl Environ Microbiol 71:5728-5734
12. John WG, Gray MR, Bates DL, Beacham JL (1993) Enzyme immunoassay-a new technique for estimating hemoglobin A1c. Clin Chem 39:663-666
13. Kobold U, Jeppsson JO, Dulffer T, Finke A, Hoelzel W, Miedema K (1997) Candidate reference methods for hemoglobin A1c based on peptide mapping. Clin Chem 43:1944-1951
14. Liao HH (1993) Thermostable mutants of kanamycin nucleotidyltransferase are also more stable to proteinase K, urea, detergents, and water-miscible organic solvents. Enzyme Microb Technol 15:286-292
15. Mrabet NT, Van den Broeck A, Van den brande I, Stanssens P, Laroche Y, Lambeir AM, Matthijssens G, Jenkins J, Chiadmi M, van Tilbeurgh H et al (1992) Arginine residues as stabilizing elements in proteins. Biochemistry 31:2239-2253
16. Nagata K, Sasaki H, Hua M, Okai M, Kubota K, Kamo M, Ito K, Ichikawa T, Koyama Y, Tanokura M (2005) Crystal structure of monomeric sarcosine oxidase from Bacillus sp. NS-129 reveals multiple conformations at the active-site loop. Proc Jpn Acad Ser B 81:220-224
17. Nanjo Y, Hayashi R, Yao T (2007) An enzymatic method for the rapid measurement of the hemoglobin A1c by a flow-injection system comprised of an electrochemical detector with a specific enzyme-reactor and a spectrophotometer. Anal Chim Acta 583:45-54
18. Sakaue R, Kajiyama N (2003) Thermostabilization of bacterial fructosyl-amino acid oxidase by directed evolution. Appl Environ Microbiol 69:139-145
19. Shapiro R, McManus MJ, Zalut C, Bunn HF (1980) Sites of nonenzymatic glycosylation of human hemoglobin A. J Biol Chem 255:3120-3127
20. Sode K, Ishimura F, Tsugawa W (2001) Screening and characterization of fructosyl-valine utilizing marine microorganism. Mar Biotechnol 3:126-132
21. Takahashi M, Pischetsrieder M, Monnier VM (1997) Molecular cloning and expression of amadoriase isoenzyme (fructosyl amine:oxygen oxidoreductase, EC 1.5.3) from Aspergillus fumigatus. J Biol Chem 272:12505-12507
22. Yanase M, Takata H, Fujii K, Takaha T, Kuriki T (2005) Cumulative effect of amino acid replacements results in enhanced thermostability of potato type L alpha-glucan phosphorylase. Appl Environ Microbiol 71:5433-5439
23. Yoshida N, Sakai Y, Isogai A, Fukuya H, Yagi M, Tani Y, Kato N (1996) Primary structures of fungal fructosyl amino acid oxidases and their application to the measurement of glycated proteins. Eur J Biochem 242:499-505
24. Yoshida N, Sakai Y, Serata M, Tani Y, Kato N (1995) Distribution and properties of fructosyl amino acid oxidase in fungi. Appl Environ Microbiol 61:4487-4489