Purification, substrate specificity, and N-terminal amino acid sequence analysis of a β-lactamase-free penicillin amidase from Alcaligenes sp.

Applied Microbiology and Biotechnology

Volumn 65, Issue 3, 2004, Pages 281-286

  Das, S ^a   Gayen, J R ^a   Pal, A ^a   Ghosh, K ^b   Rosazza, J P N ^b   Samanta, T B ^a  

^a BOSE INSTITUTE   (India)

^b UNIVERSITY OF IOWA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

6 AMINOPENICILLANIC ACID; BETA LACTAMASE; BROMINE DERIVATIVE; CEFALOTIN; DIMER; NITROGEN; PENICILLIN AMIDASE; PENICILLIN G; PHENYLACETIC ACID DERIVATIVE; TRYPTOPHAN;

AMINO ACID; ENZYME; INHIBITION;

ALCALIGENES; AMINO ACID SEQUENCE; ARTICLE; CATALYSIS; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME PURIFICATION; ENZYME SPECIFICITY; HYDROLYSIS; ISOELECTRIC POINT; NONHUMAN; PH; POLYMERIZATION; SEQUENCE ANALYSIS;

ALCALIGENES; AMINO ACID SEQUENCE; ANTI-BACTERIAL AGENTS; BETA-LACTAMASES; BETA-LACTAMS; CEPHALOTHIN; CIRCULAR DICHROISM; MOLECULAR SEQUENCE DATA; PENICILLIN AMIDASE; SEQUENCE ANALYSIS, PROTEIN; SUBSTRATE SPECIFICITY;

ALCALIGENES; ALCALIGENES FAECALIS; ALCALIGENES SP.;

EID: 4544370797     PISSN: 01757598     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00253-004-1643-1     Document Type: Article

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