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Literature summary extracted from

  • Mertens, J.A.; Braker, J.D.; Jordan, D.B.
    Catalytic properties of two Rhizopus oryzae 99-880 glucoamylase enzymes without starch binding domains expressed in Pichia pastoris (2010), Appl. Biochem. Biotechnol., 162, 2197-2213.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.2.1.3 genes amyC and amyD, expression in Pichia pastoris strain X33 Rhizopus arrhizus

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.2.1.3 maltotriose substrate inhibition of AmyC Rhizopus arrhizus
3.2.1.3 additional information AmyC, but not AmyD, exhibits substrate inhibition, the Ki for substrate inhibition decreases with increasing length of the oligosaccharides. AmyC accumulates an enzyme maltose-maltotriose dead-end complex in the steady state, kinetics and modelling, overview Rhizopus arrhizus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.2.1.3 additional information
-
additional information steady-state and pre-steady-state kinetic measurements using maltooligosacchrides as substrates, analysis and modelling, overview Rhizopus arrhizus
3.2.1.3 0.224
-
maltopentaose recombinant AmyC, pH 5.5, 40°C Rhizopus arrhizus
3.2.1.3 0.276
-
maltotetraose recombinant AmyC, pH 5.5, 40°C Rhizopus arrhizus
3.2.1.3 0.287
-
maltohexaose recombinant AmyC, pH 5.5, 40°C Rhizopus arrhizus
3.2.1.3 0.487
-
maltotriose recombinant AmyC, pH 5.5, 40°C Rhizopus arrhizus
3.2.1.3 0.53
-
maltose recombinant AmyC, pH 5.5, 40°C Rhizopus arrhizus
3.2.1.3 0.62
-
maltohexaose recombinant AmyD, pH 5.5, 40°C Rhizopus arrhizus
3.2.1.3 0.93
-
maltopentaose recombinant AmyD, pH 5.5, 40°C Rhizopus arrhizus
3.2.1.3 1.51
-
maltotetraose recombinant AmyD, pH 5.5, 40°C Rhizopus arrhizus
3.2.1.3 1.88
-
maltotriose recombinant AmyD, pH 5.5, 40°C Rhizopus arrhizus
3.2.1.3 3.78
-
maltose recombinant AmyD, pH 5.5, 40°C Rhizopus arrhizus

Organism

EC Number Organism UniProt Comment Textmining
3.2.1.3 Rhizopus arrhizus
-
two enzymes AmyC and AmyD, genes amyC or amyD
-
3.2.1.3 Rhizopus arrhizus 99-880
-
two enzymes AmyC and AmyD, genes amyC or amyD
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
3.2.1.3 glycoprotein
-
Rhizopus arrhizus

Purification (Commentary)

EC Number Purification (Comment) Organism
3.2.1.3 recombinant AmyC and AmyD from Pichia pastoris strain X33 culture supernatant by affinity chromatography, the recombinant enzymes are deglycosylated with endoglycosidase H and PNGase F Rhizopus arrhizus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.2.1.3 maltohexaose + H2O
-
Rhizopus arrhizus maltopentaose + D-glucose
-
?
3.2.1.3 maltohexaose + H2O
-
Rhizopus arrhizus 99-880 maltopentaose + D-glucose
-
?
3.2.1.3 maltopentaose + H2O
-
Rhizopus arrhizus maltotetraose + beta-D-glucose
-
?
3.2.1.3 maltopentaose + H2O
-
Rhizopus arrhizus 99-880 maltotetraose + beta-D-glucose
-
?
3.2.1.3 maltose + H2O
-
Rhizopus arrhizus beta-D-glucose + D-glucose
-
?
3.2.1.3 maltose + H2O
-
Rhizopus arrhizus 99-880 beta-D-glucose + D-glucose
-
?
3.2.1.3 maltotetraose + H2O
-
Rhizopus arrhizus maltotriose + beta-D-glucose
-
?
3.2.1.3 maltotetraose + H2O
-
Rhizopus arrhizus 99-880 maltotriose + beta-D-glucose
-
?
3.2.1.3 maltotriose + 2 H2O
-
Rhizopus arrhizus 3 beta-D-glucose
-
?
3.2.1.3 maltotriose + 2 H2O
-
Rhizopus arrhizus 99-880 3 beta-D-glucose
-
?
3.2.1.3 soluble starch + H2O
-
Rhizopus arrhizus beta-D-glucose + ?
-
?

Synonyms

EC Number Synonyms Comment Organism
3.2.1.3 alpha-1,4-glucan glucohydrolase
-
Rhizopus arrhizus
3.2.1.3 AmyC
-
Rhizopus arrhizus
3.2.1.3 AmyD
-
Rhizopus arrhizus
3.2.1.3 amyloglucosidase
-
Rhizopus arrhizus
3.2.1.3 glucoamylase
-
Rhizopus arrhizus

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.2.1.3 50
-
AmyC Rhizopus arrhizus
3.2.1.3 50
-
AmyD Rhizopus arrhizus

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.2.1.3 40
-
30 min, purified recombinant AmyC and AmyD, completely stable, rapid inactivation above Rhizopus arrhizus
3.2.1.3 50
-
30 min, inactivation of both purified recombinant AmyC and AmyD Rhizopus arrhizus

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.2.1.3 6.08
-
maltose recombinant AmyD, pH 5.5, 40°C Rhizopus arrhizus
3.2.1.3 9.3
-
maltose recombinant AmyC, pH 5.5, 40°C Rhizopus arrhizus
3.2.1.3 19.5
-
maltotriose recombinant AmyD, pH 5.5, 40°C Rhizopus arrhizus
3.2.1.3 35.1
-
soluble starch recombinant AmyD, pH 5.5, 40°C Rhizopus arrhizus
3.2.1.3 38.4
-
maltohexaose recombinant AmyD, pH 5.5, 40°C Rhizopus arrhizus
3.2.1.3 40
-
maltotetraose recombinant AmyD, pH 5.5, 40°C Rhizopus arrhizus
3.2.1.3 43.8
-
maltopentaose recombinant AmyD, pH 5.5, 40°C Rhizopus arrhizus
3.2.1.3 54.7
-
maltotriose recombinant AmyC, pH 5.5, 40°C Rhizopus arrhizus
3.2.1.3 58.2
-
soluble starch recombinant AmyC, pH 5.5, 40°C Rhizopus arrhizus
3.2.1.3 71.1
-
maltotetraose recombinant AmyC, pH 5.5, 40°C Rhizopus arrhizus
3.2.1.3 71.3
-
maltohexaose recombinant AmyC, pH 5.5, 40°C Rhizopus arrhizus
3.2.1.3 73.7
-
maltopentaose recombinant AmyC, pH 5.5, 40°C Rhizopus arrhizus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.2.1.3 5.5
-
AmyC, pH profile, overview Rhizopus arrhizus
3.2.1.3 6
-
AmyD, pH profile, overview Rhizopus arrhizus

pH Stability

EC Number pH Stability pH Stability Maximum Comment Organism
3.2.1.3 3 8 30 min, purified recombinant AmyC, 70% of maximal activity at pH 3.0, 85% at pH 8.0, profile overview Rhizopus arrhizus
3.2.1.3 3.5 8 30 min, purified recombinant AmyD, 70% of maximal activity at pH 3.5, 85% at pH 8.0, inactive at pH 3.0, profile overview Rhizopus arrhizus

General Information

EC Number General Information Comment Organism
3.2.1.3 physiological function glucoamylase enzymes catalyze hydrolysis of alpha(1-4) glycosidic bonds to release D-glucose residues from the non-reducing ends of starch and oligosaccharides. Glucoamylase also has limited ability to release D-glucose residues by promoting hydrolysis of alpha(1-6) linkages of amylopectin Rhizopus arrhizus

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
3.2.1.3 1.61
-
maltose recombinant AmyD, pH 5.5, 40°C Rhizopus arrhizus
3.2.1.3 10.4
-
maltotriose recombinant AmyD, pH 5.5, 40°C Rhizopus arrhizus
3.2.1.3 17.5
-
maltose recombinant AmyC, pH 5.5, 40°C Rhizopus arrhizus
3.2.1.3 26.5
-
maltotetraose recombinant AmyD, pH 5.5, 40°C Rhizopus arrhizus
3.2.1.3 46.9
-
maltopentaose recombinant AmyD, pH 5.5, 40°C Rhizopus arrhizus
3.2.1.3 61.9
-
maltohexaose recombinant AmyD, pH 5.5, 40°C Rhizopus arrhizus
3.2.1.3 112
-
maltotriose recombinant AmyC, pH 5.5, 40°C Rhizopus arrhizus
3.2.1.3 248
-
maltohexaose recombinant AmyC, pH 5.5, 40°C Rhizopus arrhizus
3.2.1.3 257
-
maltotetraose recombinant AmyC, pH 5.5, 40°C Rhizopus arrhizus
3.2.1.3 329
-
maltopentaose recombinant AmyC, pH 5.5, 40°C Rhizopus arrhizus