Phosphonoacetate hydrolase from Penicillium oxalicum: Purification and properties, phosphate starvation-independent expression, and partial sequencing

Research in Microbiology

Volumn 157, Issue 2, 2006, Pages 125-135

  Klimek Ochab, Magdalena ^a   Raucci, Giuseppe ^b   Lejczak, Barbara ^a   Forlani, Giuseppe ^a  

^a Department of Chemistry ^*  (Italy)

^b Menarini Ricerche SpA   (Italy)

Author keywords

Biochemical characterization; Enzyme purification; Organophosphonate degradation; Phosphonoacetate hydrolase EC 3.11.1.2 ; Phosphorus dependence; Primary structure

Indexed keywords

DIVALENT CATION; ENZYME; MONOMER; PHOSPHONOACETIC ACID; POLYCLONAL ANTIBODY;

AMINO ACID SEQUENCE; ANION EXCHANGE; ARTICLE; CHROMATOGRAPHY; ELECTROPHORESIS; ENZYME ACTIVITY; ENZYME PURIFICATION; FAST PROTEIN LIQUID CHROMATOGRAPHY; FUNGAL STRAIN; NONHUMAN; NUCLEOTIDE SEQUENCE; PENICILLIUM; PENICILLIUM OXALICUM; PH; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN PURIFICATION; SENSITIVITY ANALYSIS; WILD TYPE;

AMINO ACID SEQUENCE; CHROMATOGRAPHY, LIQUID; ENZYME ACTIVATORS; ENZYME INHIBITORS; ENZYME STABILITY; GENE EXPRESSION REGULATION, FUNGAL; HYDROGEN-ION CONCENTRATION; MASS SPECTROMETRY; METALS; MOLECULAR SEQUENCE DATA; MOLECULAR WEIGHT; PENICILLIUM; PHOSPHORIC MONOESTER HYDROLASES; SEQUENCE HOMOLOGY, AMINO ACID;

BACTERIA (MICROORGANISMS); PENICILLIUM; PENICILLIUM OXALICUM;

EID: 32644432880     PISSN: 09232508     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.resmic.2005.06.002     Document Type: Article

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