TY - JOUR
T1 - Partial purification and properties of putrescine oxidase from Candida guilliermondii
AU - Gunasekaran, Muthukumaran
AU - Gunasekaran, Uma
N1 - Funding Information:
The authors are grateful to Ms. Loretta Kellogg for technical assistance. This study was supported in part by the National Science Foundation grant HRD 92-53037, the Kellogg Foundation grant P0010125, the Howard Hughes Medical Institute grant 71194-527802, and the Department of Education grant P-120A30013.
PY - 1999
Y1 - 1999
N2 - Putrescine oxidase ([PO]; E.C. 1.4.3.4), which catalyzes the oxidative deamination of putrescine into γ-aminobutyraldehyde, has been partially purified from Candida guilliermondii. Among the substrates tested, putrescine has the highest reaction rate, followed by spermidine and cadaverine. The K(m) values for putrescine, spermidine, and cadaverine were 20, 200, and 1.1 mM, respectively. The optimum pH and the temperature for PO were 8.0 and 37°C, respectively. Growth of Candida species on putrescine as the sole nitrogen source induced the synthesis of PO that converts putrescine into Δ1-pyrroline and γ-aminobutyric acid. These two products were detected and identified from the culture medium. The enzyme was not activated by divalent cations. Among the species of Candida tested, the highest enzyme activity was found in cell-free extracts of C. guilliermondii. The pathway of putrescine degradation was identified by substrate analysis to be along the nonacetylated pathway in C. guilliermondii.
AB - Putrescine oxidase ([PO]; E.C. 1.4.3.4), which catalyzes the oxidative deamination of putrescine into γ-aminobutyraldehyde, has been partially purified from Candida guilliermondii. Among the substrates tested, putrescine has the highest reaction rate, followed by spermidine and cadaverine. The K(m) values for putrescine, spermidine, and cadaverine were 20, 200, and 1.1 mM, respectively. The optimum pH and the temperature for PO were 8.0 and 37°C, respectively. Growth of Candida species on putrescine as the sole nitrogen source induced the synthesis of PO that converts putrescine into Δ1-pyrroline and γ-aminobutyric acid. These two products were detected and identified from the culture medium. The enzyme was not activated by divalent cations. Among the species of Candida tested, the highest enzyme activity was found in cell-free extracts of C. guilliermondii. The pathway of putrescine degradation was identified by substrate analysis to be along the nonacetylated pathway in C. guilliermondii.
KW - Candida sp.
KW - Enzyme purification
KW - Polyamines
KW - Spermidine
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U2 - 10.1385/ABAB:76:3:229
DO - 10.1385/ABAB:76:3:229
M3 - Article
C2 - 10390812
AN - SCOPUS:0033014712
SN - 0273-2289
VL - 76
SP - 229
EP - 236
JO - Applied Biochemistry and Biotechnology - Part A Enzyme Engineering and Biotechnology
JF - Applied Biochemistry and Biotechnology - Part A Enzyme Engineering and Biotechnology
IS - 3
ER -