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Literature summary for 3.2.1.20 extracted from

  • Ernst, H.A.; Lo Leggio, L.; Willemoes, M.; Leonard, G.; Blum, P.; Larsen, S.
    Structure of the Sulfolobus solfataricus alpha-glucosidase: implications for domain conservation and substrate recognition in GH31 (2006), J. Mol. Biol., 358, 1106-1124.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
gene malA, DNA and amino acid sequence analysis, phylogenetic tree, overexpression of wild-type and selenomethionine-labeled enzyme in Escherichia coli strain NF1830 Saccharolobus solfataricus

Crystallization (Commentary)

Crystallization (Comment) Organism
purified recombinant wild-type and selenomethionine-labeled enzyme, hanging drop vapour diffusion method, hexameric crystal form, X-ray diffraction structure determination and analysis of the different crystal forms at 2.5 A resolution, structure modelling of domains, full-length enzyme, and active site Saccharolobus solfataricus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information kinetics Saccharolobus solfataricus
2
-
4-nitrophenyl alpha-D-glucopyranoside pH 4.5, 85°C, recombinant enzyme Saccharolobus solfataricus

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
470000
-
recombinant enzyme, native PAGE Saccharolobus solfataricus
480000
-
recombinant enzyme, gel filtration Saccharolobus solfataricus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
maltose + H2O Saccharolobus solfataricus
-
alpha-D-glucose + D-glucose
-
?

Organism

Organism UniProt Comment Textmining
Saccharolobus solfataricus P0CD66 gene malA
-

Purification (Commentary)

Purification (Comment) Organism
recombinant wild-type and selenomethionine-labeled enzyme from Escherichia coli strain NF1830 by ammonium sulfate fractionation, ion exchange chromatography, and gel filtration Saccharolobus solfataricus

Reaction

Reaction Comment Organism Reaction ID
maltotetraose + 3 H2O = 4 alpha-D-glucose substrate recognition and catalytic mechanism, active site structure, residues R400, D87, W284, M321, F327 are involved in formation of the +1 subsite in the GH31 alpha-glucosidase substrate binding Saccharolobus solfataricus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4-nitrophenyl alpha-D-glucopyranoside + H2O
-
Saccharolobus solfataricus 4-nitrophenol + alpha-D-glucose
-
?
maltose + H2O
-
Saccharolobus solfataricus alpha-D-glucose + D-glucose
-
?
maltose + H2O preferred substrate, Asp251 and Trp284 interact with the position 6 OH group of the substrate Saccharolobus solfataricus alpha-D-glucose + D-glucose
-
?
additional information substrate specificity, overview Saccharolobus solfataricus ?
-
?

Subunits

Subunits Comment Organism
hexamer domain structure analysis, quarternary organization, comparison to alpha-xylosidase Yic1 Saccharolobus solfataricus
More monomer fold, overview Saccharolobus solfataricus

Synonyms

Synonyms Comment Organism
AG
-
Saccharolobus solfataricus
MalA
-
Saccharolobus solfataricus
More the enzyme belongs to the glycoside hydrolase family 31, GH31 Saccharolobus solfataricus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
85
-
assay at Saccharolobus solfataricus

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
33
-
4-nitrophenyl alpha-D-glucopyranoside pH 4.5, 85°C, recombinant enzyme Saccharolobus solfataricus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
4.5
-
assay at Saccharolobus solfataricus