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PMID:11734885

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Citation

Frankowski, J, Lorito, M, Scala, F, Schmid, R, Berg, G and Bahl, H (2001) Purification and properties of two chitinolytic enzymes of Serratia plymuthica HRO-C48. Arch. Microbiol. 176:421-6

Abstract

The chitinolytic rhizobacterium Serratia plymuthica HRO-C48 was previously selected as a biocontrol agent of phytopathogenic fungi. One endochitinase (E.C. 3.2.1.14), CHIT60, and one N-acetyl-beta-1,4- D-hexosaminidase (E.C. 3.2.1.52), CHIT100, were purified and characterized. The endochitinase CHIT60, with an apparent molecular mass of 60.5 kDa, had a N-terminal amino acid sequence highly similar to that of chitinases A from Serratia liquefaciens and Serratia marcescens. The enzyme activity had its peak at 55 degrees C and pH 5.4, and increased by more than 20% in the presence of 10 mM Ca(2+), Co(2+) or Mn(2+). Activity was inhibited by 80% in the presence of 10 mM Cu(2+). CHIT100 appeared to be a monomeric enzyme with a molecular mass of 95.6 kDa and a pI of 6.8. Optimal activity was obtained at 43 degrees C and pH 6.6, and decreased by more than 90 % in the presence of 10 mM Co(2+) or Cu(2+). CHIT100 (100 microg ml(-1)) inhibited spore germination and germ tube elongation of the phytopathogenic fungus Botrytis cinerea by 28 % and 31.6 %, respectively. With CHIT60 (100 microg ml(-1)), the effect was more pronounced: 78 % inhibition of of germination and 63.9 % inhibition of germ tube elongation.

Links

PubMed Online version:10.1007/s002030100347

Keywords

Amino Acid Sequence; Botrytis/drug effects; Chitinase/chemistry; Chitinase/genetics; Chitinase/isolation & purification; Cloning, Molecular; Genes, Bacterial; Hydrogen-Ion Concentration; Molecular Sequence Data; Molecular Weight; Sequence Alignment; Serratia/enzymology; Serratia/genetics; Temperature; beta-N-Acetylhexosaminidases/chemistry; beta-N-Acetylhexosaminidases/genetics; beta-N-Acetylhexosaminidases/isolation & purification

Significance

Annotations

Gene product Qualifier GO Term Evidence Code with/from Aspect Extension Notes Status

SERPL:Q8KKF5

enables

GO:0008843: endochitinase activity

ECO:0000314: direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

SERPL:Q8KKF5

GO:0008843: endochitinase activity

ECO:0000314:

F

Figure 3 depicts the optimum temperature and pH for endochitinase activity.

complete
CACAO 7753


See also

References

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