Purification and Properties of a Glucuronan Lyase from Sinorhizobium meliloti M5N1CS (NCIMB 40472)
2001 ◽
Vol 67
(11)
◽
pp. 5197-5203
◽
Keyword(s):
ABSTRACT A glucuronan lyase extracted from Sinorhizobium meliloti strain M5N1CS was purified to homogeneity by anion-exchange chromatography. The purified enzyme corresponds to a monomer with a molecular mass of 20 kDa and a pI of 4.9. A specific activity was found only for polyglucuronates leading to the production of 4,5-unsaturated oligoglucuronates. The enzyme activity was optimal at pH 6.5 and 50°C. Zn2+, Cu2+, and Hg2+ (1 mM) inhibited the enzyme activity. No homology of the enzyme N-terminal amino acid sequence was found with any of the previously published protein sequences. This enzyme purified fromS. meliloti strain M5N1CS corresponding to a new lyase was classified as an endopolyglucuronate lyase.
2002 ◽
Vol 57
(11-12)
◽
pp. 1042-1046
◽
1979 ◽
Vol 34
(9-10)
◽
pp. 721-725
◽
1998 ◽
Vol 64
(8)
◽
pp. 2920-2924
◽
1981 ◽
Vol 46
(8)
◽
pp. 1994-2004
◽
1998 ◽
Vol 180
(20)
◽
pp. 5351-5356
◽
1979 ◽
Vol 34
(1-2)
◽
pp. 27-32
◽
1974 ◽
Vol 39
(7)
◽
pp. 1933-1939
Keyword(s):
1980 ◽
Vol 45
(4)
◽
pp. 1144-1154
◽
Keyword(s):
1991 ◽
Vol 266
(11)
◽
pp. 7044-7050
Keyword(s):