The invariant F283 and its strategic position in the hydrophobic cleft of streptomyces jumonjinensis isopenicillin N synthase active site are functionally important

Biochemical and Biophysical Research Communications

Volumn 283, Issue 3, 2001, Pages 621-626

  Wong, Esther ^a   Sim, Janet ^a   Sim, Tiow Suan ^a  

^a NATIONAL UNIVERSITY OF SINGAPORE   (Singapore)

Author keywords

Deacetoxycephalosporin C synthase; Hydrophobic cavity; Isopenicillin N synthase; Phenylalanine; Site directed mutagenesis

Indexed keywords

AMINO ACID; IRON BINDING PROTEIN; ISOPENICILLIN N SYNTHETASE; PHENYL GROUP; PHENYLALANINE;

ARTICLE; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME STRUCTURE; GENE MUTATION; HYDROPHOBICITY; NONHUMAN; PRIORITY JOURNAL; STREPTOMYCES; STREPTOMYCES JUMOJINENSIS;

EID: 0034811575     PISSN: 0006291X     EISSN: None     Source Type: Journal    
DOI: 10.1006/bbrc.2001.4781     Document Type: Article

References (19)

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3. Structure of isopenicillin N synthase complexed with substrate and the mechanism of penicillin formation
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9. Protein modeling for all
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11. Mutational analysis of tyrosine-191 in the catalysis of Cephalosporium acremonium isopenicillin N synthase
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13. Biophysical factors affecting the expression of isopenicillin N synthase isozymes in Escherichia coli
14. Cleavage of structural proteins during the assembly of the head of bacteriophage T4
15. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
16. Mutational evidence supporting the involvement of tripartite residues His183, Asp185 and His243 in Streptomyces clavuligerus deacetoxycephalosporin C synthase for catalysis
17. Structure of cephalosporin synthase
18. An active site phenylalanine of 3-oxo-delta 5-steriod isomerase is catalytically important for proton transfer
19. Metal-binding specificity in carbonic anhydrase is influenced by conserved hydrophobic core residues