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Literature summary for 4.2.2.23 extracted from

  • McKie, V.A.; Vincken, J.P.; Voragen, A.G.; van den Broek, L.A.; Stimson, E.; Gilbert, H.J.
    A new family of rhamnogalacturonan lyases contains an enzyme that binds to cellulose (2001), Biochem. J., 355, 167-177.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli. Expression of the three modules of the Pseudomonas protein in Escherichia coli shows that its C-terminal module is a functional cellulose-binding domain, and the N-terminal module consists of a catalytic domain that hydrolyzes rhamnogalacturonan-containing substrates Cellvibrio japonicus

General Stability

General Stability Organism
completely resistant to proteinase attack Cellvibrio japonicus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
potato pectic galactan KM-value: 8.5 mg/ml at pH 9.5 Cellvibrio japonicus

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ absolute requirement for calcium Cellvibrio japonicus

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
93415
-
x * 93415, calculated from sequence Cellvibrio japonicus

Organism

Organism UniProt Comment Textmining
Cellvibrio japonicus Q9AF09
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
potato pectic galactan apple-derived and potato-derived rhamnogalacturonan substrates. The enzyme has a strong preference for rhamnogalacturonans that contain galactose side chains, and which are not esterified. The increase in absorbance at 235 nm indicates that glycosidic bond cleavage is mediated via a beta-elimination mechanism Cellvibrio japonicus potato pectic galactan oligosaccharides
-
?
rhamnogalacturonan I apple-derived and potato-derived rhamnogalacturonan substrates. The enzyme has a strong preference for rhamnogalacturonans that contain galactose side chains, and which are not esterified. The increase in absorbance at 235 nm indicates that glycosidic bond cleavage is mediated via a beta-elimination mechanism Cellvibrio japonicus rhamnogalacturonan I oligosaccharides with alpha-L-rhamnopyranose at the reducing end and 4-deoxy-4,5-unsaturated D-galactopyranosyluronic acid at the nonreducing end
-
?

Subunits

Subunits Comment Organism
? x * 93415, calculated from sequence Cellvibrio japonicus

Synonyms

Synonyms Comment Organism
Rgl11A
-
Cellvibrio japonicus

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
55
-
10 min, about 5% loss of activity Cellvibrio japonicus
60
-
10 min, about 40% loss of activity Cellvibrio japonicus
65
-
10 min, about 65% loss of activity Cellvibrio japonicus

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
additional information
-
potato pectic galactan kcat-value: 6500/s at pH 9.5 Cellvibrio japonicus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
9.5
-
-
Cellvibrio japonicus

pH Range

pH Minimum pH Maximum Comment Organism
8.5 10.5 pH 8.5: about 60% of maximal activity, pH 10.5: about about 40% of maximal activity Cellvibrio japonicus