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Literature summary for 3.2.1.174 extracted from

  • Matsumoto, S.; Yamada, H.; Kunishige, Y.; Takenaka, S.; Nakazawa, M.; Ueda, M.; Sakamoto, T.
    Identification of a novel Penicillium chrysogenum rhamnogalacturonan rhamnohydrolase and the first report of a rhamnogalacturonan rhamnohydrolase gene (2017), Enzyme Microb. Technol., 98, 76-85 .
    View publication on PubMed
Search for more literature for 3.2.1.174

Activating Compound

Activating Compound Comment Organism Structure
additional information EDTA has no significant effect on enzyme activity Penicillium chrysogenum

Cloned(Commentary)

Cloned (Comment) Organism
gene Pcrgrh78A, DNA and amino acid sequence determination and analysis, phylogenetic analysis, recombinant overexpression in Aspergillus oryzae strain niaD300, subcloning in Escherichia coli strain DH5alpha Penicillium chrysogenum

Inhibitors

Inhibitors Comment Organism Structure
Ag+
-
 Penicillium chrysogenum
Cu2+
-
 Penicillium chrysogenum
Fe3+
-
 Penicillium chrysogenum
Hg2+
-
 Penicillium chrysogenum
L-rhamnose 50% inhibition at 50 mM Penicillium chrysogenum
additional information EDTA has no significant effect on enzyme activity Penicillium chrysogenum

Localization

Localization Comment Organism GeneOntology No. Textmining
extracellular
-
 Penicillium chrysogenum
-
-

Metals/Ions

Metals/Ions Comment Organism Structure
additional information Ba2+, Ca2+, Cd2+, Co2+, Fe2+, K+, Mn2+, Na+, Ni2+, and Zn2+ have no significant effect on the enzyme activity Penicillium chrysogenum

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
96000
-
 recombinant enzyme, gel filtration Penicillium chrysogenum

Organism

Organism UniProt Comment Textmining
Penicillium chrysogenum A0A110AZ24 i.e. Penicillium notatum
-
Penicillium chrysogenum 31B A0A110AZ24 i.e. Penicillium notatum
-

Posttranslational Modification

Posttranslational Modification Comment Organism
glycoprotein the native extracellular enzyme is N-linked glycosylated, deglycosylation with endoglycosidase H. Fifteen asparagine residues in PcR-GRH78A are identified as possible N-glycosylation sites Penicillium chrysogenum

Purification (Commentary)

Purification (Comment) Organism
native extracellular enzyme from Penicillium chrysogenum strain 31B and recombinant enzyme expressed in Aspergillus oryzae strain niaD300 both about 10fold by ultrafiltration, ammonium sulfate fractionation, anion exchange chromatography, and two different steps of hydrophobic interaction chromatography, followed by dialysis and gel filtration Penicillium chrysogenum

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
39.6
-
 purified recombinant enzyme, pH 5.0, 37°C Penicillium chrysogenum

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information enzyme PcRGRH78A specifically hydrolyzes rhamnogalacturonan oligosaccharides that contain rhamnose at their nonreducing ends, releasing the L-rhamnose, but it has no activity toward naringin, hesperidin,or rutin. When galactosyl rhamnogalacturonan oligosaccharides are used as substrate, PcRGRH78A releases Rha in 3.5fold greater amounts in the presence of beta-galactosidase than in its absence, indicating that PcRGRH78A preferentially acts on Rha residues without the galactose moietyat nonreducing ends Penicillium chrysogenum ?
-
 ?
additional information enzyme PcRGRH78A specifically hydrolyzes rhamnogalacturonan oligosaccharides that contain rhamnose at their nonreducing ends, releasing the L-rhamnose, but it has no activity toward naringin, hesperidin,or rutin. When galactosyl rhamnogalacturonan oligosaccharides are used as substrate, PcRGRH78A releases Rha in 3.5fold greater amounts in the presence of beta-galactosidase than in its absence, indicating that PcRGRH78A preferentially acts on Rha residues without the galactose moietyat nonreducing ends Penicillium chrysogenum 31B ?
-
 ?
rhamnogalacturonan oligosaccharide + H2O two oligosaccharides, RG4 (Rha-GalA-Rha-GalA: RG4) and the RG hexasaccharide (Rha-GalA-Rha-GalA-Rha-GalA: RG6), prepared from potato rhamnogalacturonan I Penicillium chrysogenum L-rhamnose + ?
-
 ?
rhamnogalacturonan oligosaccharide + H2O two oligosaccharides, RG4 (Rha-GalA-Rha-GalA: RG4) and the RG hexasaccharide (Rha-GalA-Rha-GalA-Rha-GalA: RG6), prepared from potato rhamnogalacturonan I Penicillium chrysogenum 31B L-rhamnose + ?
-
 ?

Subunits

Subunits Comment Organism
monomer 1 * 82000, glycosylated enzyme, SDS-PAGE, 1 * 67000, deglycosylated enzyme, SDS-PAGE, 1 * 101000, recombinant enzyme, SDS-PAGE Penicillium chrysogenum
More peptide mapping Penicillium chrysogenum

Synonyms

Synonyms Comment Organism
alpha-L-rhamnosidase
-
 Penicillium chrysogenum
PcRGRH78A
-
 Penicillium chrysogenum
RG rhamnohydrolase
-
 Penicillium chrysogenum
RGRH
-
 Penicillium chrysogenum

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
 assay at Penicillium chrysogenum

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
5
-
 assay at Penicillium chrysogenum

General Information

General Information Comment Organism
evolution the enzyme belongs to the glycoside hydrolase family 78, GH78, group 3. Enzyme PcRGRH78A contains a bacterial alpha-L-rhamnosidase (PF05592) domain, but shows no activity with rhamnogalacturonan oligosaccharides Penicillium chrysogenum