Pectate lyase is responsible for the eliminative cleavage of pectate, yielding oligosaccharides with 4-deoxy-?-D-mann-4-enuronosyl groups at their non-reducing ends.
12.
Pectate lyase is responsible for the eliminative cleavage of pectate, yielding oligosaccharides with 4-deoxy-?-D-mann-4-enuronosyl groups at their non-reducing ends.
13.
The structure and the folding kinetics of one member of this family, pectate lyase C ( " pelC " ) 1 from Erwinia chrysanthemi has been investigated in some detail,.
14.
For example, a mutation disabled an " Arabidopsis " gene encoding pectate lyase ( involved in cell wall degradation ), conferring resistance to the powdery mildew pathogen " Golovinomyces cichoracearum ".
15.
The first beta-helix was observed in the enzyme pectate lyase, which contains a seven-turn helix that reaches 34 ?( 3.4 trimer is 200 ?( 20 nm ) in length.
16.
I, a major allergenic glycoprotein of " Cryptomeria japonica " ( Japanese cedar ) the most common pollen allergen in Japan; and P56 and P59, which share sequence similarity with pectate lyases of plant pathogenic bacteria.
17.
""'Telluria mixta " "'( formerly called " Pseudomonas mixta " ) is a species of Gram-negative soil bacteria that actively degrades polysaccharides including dextran, inulin, pectate, starch, and xylan.
18.
II family include " Tobacco " ( " Nicotiana tabacum ", Common tobacco ) pectate lyase, which is similar to the deduced amino acid sequences of two pollen-specific pectate lyase genes identified in " Lycopersicon esculentum " ( Tomato ); " Cry j"
19.
II family include " Tobacco " ( " Nicotiana tabacum ", Common tobacco ) pectate lyase, which is similar to the deduced amino acid sequences of two pollen-specific pectate lyase genes identified in " Lycopersicon esculentum " ( Tomato ); " Cry j"
20.
"Erwinia carotovora " is a plant pathogen that causes soft rot in a number of crops such as potatoes and carrots by using N-hexanoyl-l-HSL ( C6-HSL ) quorom sensing to evade the plant's defense systems and coordinate its production of pectate lyase during the infection process.
