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Literature summary for 3.2.1.20 extracted from

  • Ferrer, M.; Golyshina, O.V.; Plou, F.J.; Timmis, K.N.; Golyshin, P.N.
    A novel alpha-glucosidase from the acidophilic archaeon Ferroplasma acidiphilum strain Y with high transglycosylation activity and an unusual catalytic nucleophile (2005), Biochem. J., 391, 269-276.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.2.1.20

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Ferroplasma acidiphilum

Protein Variants

Protein Variants Comment Organism
H243A kcat/Km is 23% lower than wild-type value, the iron content is about 55% compared to wild-type enzyme Ferroplasma acidiphilum
H275A kcat/Km is slighly higher than wild-type value, the iron content is similar to that of the wild-type enzyme Ferroplasma acidiphilum
H277A kcat/Km is slighly lower than wild-type value, the iron content is similar to that of the wild-type enzyme Ferroplasma acidiphilum
H325A kcat/Km is slighly higher than wild-type value, the iron content is similar to that of the wild-type enzyme Ferroplasma acidiphilum
H390A kcat/Km is 98% lower than wild-type value, contains no iron Ferroplasma acidiphilum
H41A kcat/Km is slighly higher than wild-type value, the iron content is similar to that of the wild-type enzyme Ferroplasma acidiphilum
H47A kcat/Km is 25% lower than wild-type value, the iron content is about 85% compared to wild-type enzyme Ferroplasma acidiphilum
H9A kcat/Km is slighly higher than wild-type value, the iron content is similar to that of the wild-type enzyme Ferroplasma acidiphilum

Inhibitors

Inhibitors Comment Organism Structure
5-fluoro-alpha-D-glucopyranosyl fluoride strong inhibition by the reversible inhibitor, which inhibits immediately upon addition and maintains the same level of inhibition over time Ferroplasma acidiphilum
diethyl dicarbonate
-
 Ferroplasma acidiphilum
additional information no inactivation with 1-ethyl-3-[3-(dimethylamino)propyl]carbodi-imide, tetranitromethane, N-ethylmaleimide, iodoacetate, p-chloromercuribenzoate, 4-chloromercuriphenylsulfonic acid, di-isopropyl fluorophosphate, PMSF. The presence of glucose and maltose, the end-products of the hydrolysis of sucrose, maltose and maltotriose, does not affect the hydrolytic activity of the enzyme Ferroplasma acidiphilum
tosylphenylalanylchloromethane
-
 Ferroplasma acidiphilum

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.32
-
 sucrose pH 3.0, 50°C, wild-type enzyme Ferroplasma acidiphilum
0.64
-
 maltose pH 3.0, 50°C, wild-type enzyme Ferroplasma acidiphilum
0.69
-
 maltotriose pH 3.0, 50°C, wild-type enzyme Ferroplasma acidiphilum
5
-
 4-nitrophenyl alpha-D-glucopyranoside pH 3.0, 50°C, wild-type enzyme Ferroplasma acidiphilum
9.3
-
 maltotetraose pH 3.0, 50°C, wild-type enzyme Ferroplasma acidiphilum

Metals/Ions

Metals/Ions Comment Organism Structure
Iron the enzyme contains 1.04 mol of iron per mol of enzyme Ferroplasma acidiphilum

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
57000
-
 x * 57000, SDS-PAGE Ferroplasma acidiphilum
57300
-
 x * 57300, calculated from sequence Ferroplasma acidiphilum

Organism

Organism UniProt Comment Textmining
Ferroplasma acidiphilum Q5K3Q3
-
-
Ferroplasma acidiphilum DSM 12658 Q5K3Q3
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4-nitrophenyl alpha-D-glucopyranoside + H2O
-
 Ferroplasma acidiphilum 4-nitrophenol + alpha-D-glucose
-
 ?
maltose + H2O
-
 Ferroplasma acidiphilum 2 D-glucose
-
 ?
maltose + H2O
-
 Ferroplasma acidiphilum DSM 12658 2 D-glucose
-
 ?
maltotetraose + H2O very low activity Ferroplasma acidiphilum ?
-
 ?
maltotetraose + H2O very low activity Ferroplasma acidiphilum DSM 12658 ?
-
 ?
maltotriose + H2O
-
 Ferroplasma acidiphilum ?
-
 ?
maltotriose + H2O
-
 Ferroplasma acidiphilum DSM 12658 ?
-
 ?
additional information the enzyme also shows high transglycosylation activity, it transfers glucosyl groups from maltose to produce maltotriose selectively Ferroplasma acidiphilum ?
-
 ?
additional information the enzyme also shows high transglycosylation activity, it transfers glucosyl groups from maltose to produce maltotriose selectively Ferroplasma acidiphilum DSM 12658 ?
-
 ?
sucrose + H2O
-
 Ferroplasma acidiphilum D-glucose + D-fructose
-
 ?
sucrose + H2O
-
 Ferroplasma acidiphilum DSM 12658 D-glucose + D-fructose
-
 ?

Subunits

Subunits Comment Organism
? x * 57000, SDS-PAGE Ferroplasma acidiphilum
? x * 57300, calculated from sequence Ferroplasma acidiphilum

Synonyms

Synonyms Comment Organism
alphaGluFa
-
 Ferroplasma acidiphilum

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
50
-
 assay at Ferroplasma acidiphilum
55 60 hydrolysis of sucrose Ferroplasma acidiphilum

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
50
-
 pH 2.5, t1/2: 34 min Ferroplasma acidiphilum
55
-
 thermostability: 57 min Ferroplasma acidiphilum
60
-
 thermostability: 32 vmin Ferroplasma acidiphilum
65
-
 thermostability: less than 5 min Ferroplasma acidiphilum

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2.8
-
 maltotetraose pH 3.0, 50°C, wild-type enzyme Ferroplasma acidiphilum
13
-
 maltotriose pH 3.0, 50°C, wild-type enzyme Ferroplasma acidiphilum
22.5
-
 4-nitrophenyl alpha-D-glucopyranoside pH 3.0, 50°C, wild-type enzyme Ferroplasma acidiphilum
94
-
 sucrose pH 3.0, 50°C, wild-type enzyme Ferroplasma acidiphilum
126
-
 maltose pH 3.0, 50°C, wild-type enzyme Ferroplasma acidiphilum

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
2.4 3.5 hydrolysis of sucrose Ferroplasma acidiphilum
3
-
 assay at Ferroplasma acidiphilum

pH Range

pH Minimum pH Maximum Comment Organism
1.5 6 pH 1.5: 74% of maximal activity, pH 2.0: 92% of maximal activity, pH 6.0: about 35% of maximal activity. No measurable activity is detected at pH values above 7.0 and below 1.0 Ferroplasma acidiphilum

pH Stability

pH Stability pH Stability Maximum Comment Organism
2.5
-
 50°C, t1/2: 34 min Ferroplasma acidiphilum

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.0029
-
 diethyl dicarbonate pH 3.0, 50°C Ferroplasma acidiphilum
0.0042
-
 tosylphenylalanylchloromethane pH 3.0, 50°C Ferroplasma acidiphilum

pI Value

Organism Comment pI Value Maximum pI Value
Ferroplasma acidiphilum calculated from sequence
-
 6.42

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
0.3
-
 maltotetraose pH 3.0, 50°C, wild-type enzyme Ferroplasma acidiphilum
4.5
-
 4-nitrophenyl alpha-D-glucopyranoside pH 3.0, 50°C, wild-type enzyme Ferroplasma acidiphilum
5.4
-
 sucrose pH 3.0, 50°C, mutant enzyme H390A Ferroplasma acidiphilum
18.8
-
 maltotriose pH 3.0, 50°C, wild-type enzyme Ferroplasma acidiphilum
197
-
 maltose pH 3.0, 50°C, wild-type enzyme Ferroplasma acidiphilum
220
-
 sucrose pH 3.0, 50°C, mutant enzyme H47A Ferroplasma acidiphilum
227
-
 sucrose pH 3.0, 50°C, mutant enzyme H243A Ferroplasma acidiphilum
291
-
 sucrose pH 3.0, 50°C, mutant enzyme H277A Ferroplasma acidiphilum
293
-
 sucrose pH 3.0, 50°C, wild-type enzyme Ferroplasma acidiphilum
296
-
 sucrose pH 3.0, 50°C, mutant enzyme H325A Ferroplasma acidiphilum
297
-
 sucrose pH 3.0, 50°C, mutant enzyme H275A Ferroplasma acidiphilum
302
-
 sucrose pH 3.0, 50°C, mutant enzyme H9A Ferroplasma acidiphilum
312
-
 sucrose pH 3.0, 50°C, mutant enzyme H41A Ferroplasma acidiphilum