Aromatic L-amino acid decarboxylase: Conformational change in the flexible region around Arg334 is required during the transaldimination process

Protein Science

Volumn 7, Issue 8, 1998, Pages 1802-1810

  Ishii, Seiji ^a   Hayashi, Hideyuki ^a   Okamoto, Akihiro ^a   Kagamiyama, Hiroyuki ^a  

^a OSAKA MEDICAL COLLEGE   (Japan)

Author keywords

Aromatic L amino acid decarboxylase; Conformational change; Differential chemical modification; Fragmentary enzyme; Limited proteolysis; Pyridoxal 5' phosphate; Transaldimination

Indexed keywords

ARGININE; AROMATIC LEVO AMINO ACID DECARBOXYLASE; CHYMOTRYPSIN; DIHYDROXYPHENYLACETIC ACID; ESTER DERIVATIVE; LEVODOPA; PHENYLACETIC ACID DERIVATIVE; PROTEINASE; SULFONIC ACID DERIVATIVE; TRYPSIN;

ARTICLE; CATALYSIS; CHEMICAL MODIFICATION; CONFORMATIONAL TRANSITION; ENZYME ACTIVITY; ENZYME ANALYSIS; ENZYME CONFORMATION; ENZYME MODIFICATION; ENZYME SUBSTRATE COMPLEX; PRIORITY JOURNAL; PROTEIN EXPRESSION; SPECTROPHOTOMETRY; STEADY STATE; STRUCTURE ACTIVITY RELATION;

EID: 0032456134     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1002/pro.5560070816     Document Type: Article

References (17)

1. Antson AA, Demidkina TV, Gollnick P, Dauter Z, Von Tersch RL, Long J, Berezhnoy SN, Phillips RS, Harutyunyan EH, Wilson KS. 1993. Three-dimensional structure of tyrosine phenol-lyase. Biochemistry 32:4195-4206.
2. Arnone A, Rogers PH, Hyde CC, Briley PD, Metzler CM, Metzler DE. 1985. Pig cytosolic aspartate aminotransferase: The structures of the internal aldimine, external aldimine, and ketimine and of the β subform. In: Christen P, Metzler DE, eds. Transaminases, New York: John Wiley and Sons, pp 138-154.
3. Bottomley JR, Hawkins AR, Kleanthous C. 1996. Conformational changes and the role of metals in the mechanism of type II dehydroquinase from Aspergillus nidulans. Biochem J 319:269-278.
4. Clausen T, Huber R, Laber B, Pohlenz HD, Messerschmidt A. 1996. Crystal structure of the pyridoxal-5′-phosphate dependent cystathionine β-lyase from Escherichia coli at 1.83 Å. J Mol Biol 262:202-224.
5. Crestfield AM, Moore S, Stein WH. 1963. The preparation and enzymatic hydrolysis of reduced and S-carboymethylated proteins. J Biol Chem 238:622-627.
6. Davis BJ. 1964. Method and application to human serum proteins. Ann NY Acad Sci 121:404-427.
7. Fetrow JS. 1995. Omega loops: Nonregular secondary structures significant in protein function and stability. FASEB J 9:708-717.
8. First EA, Fersht AR. 1993. Mutational and kinetic analysis of a mobile loop in tyrosyl-tRNA synthetase. Biochemistry 32:13658-13663.
9. Fontana A. 1989. Limited proteolysis of globular proteins occurs at exposed and flexible loops. In: Kotyk A, Skoda J, Paces V, Kostka V, eds. Hilights of modern biochemistry. Utrecht, The Netherlands: VSP International Science Publishers, pp 1711-1726.
10. Fontana A, Zambonin M, Polverino dLP, De FV, Clementi A, Scaramella E. 1997. Probing the conformational state of apomyoglobin by limited proteolysis. J Mol Biol 266:223-230.
11. Grishin NV, Phillips MA, Goldsmith EJ. 1995. Modeling of the spatial structure of eukaryotic ornithine decarboxylases. Protein Sci 4:1291-1304.
12. Hayashi H, Mizuguchi H, Kagamiyama H. 1993. Rat liver aromatic L-amino acid decarboxylase: Spectroscopic and kinetic analysis of the coenzyme and reaction intermediates. Biochemistry 32:812-818.
13. Hubbard SJ, Eisenmenger F, Thornton JM. 1994. Modeling studies of the change in conformation required cleavage of limited proteolytic sites. Protein Sci 3:757-768.
14. Ishii S, Mizuguchi H, Nishino J, Hayashi H, Kagamiyama H. 1996. Functionally important residues of aromatic L-amino acid decarboxylase probed by sequence alignment and site-directed mutagenesis. J Biochem 120:369-376.
15. Isupov MN, Antson AA, Dodson EJ, Dodson GG, Dementieva IS, Zakomirdina LN, Wilson KS, Dauter Z, Lebedev AA, Harutyunyan EH. 1998. Crystal structure of tryptophanase. J Mol Biol 276:603-623.
16. Jansonius JN, Eichele G, Ford GC, Picot D, Thaller C, Vincent M. 1985. Spatial structure of mitochondrial aspartate aminotransferase. In: Christen P, Metzler DE, eds. Transaminases. New York: John Wiley and Sons, pp 109-137.
17. Joseph D, Petsko GA, Karplus M. 1990. Anatomy of a conformational change: Hinged "lid" motion of the triosephosphate isomerase loop. Science 249:1425-1428.