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Literature summary extracted from

  • Kaper, T.; van Heusden, H.H.; van Loo, B.; Vasella, A.; van der Oost, J.; de Vos, W.M.
    Substrate specificity engineering of beta-mannosidase and beta-glucosidase from Pyrococcus by exchange of unique active site residues (2002), Biochemistry, 41, 4147-4155.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.2.1.25 expression in Escherichia coli Pyrococcus horikoshii
3.2.1.B28 expression in Escherichia coli Pyrococcus furiosus

Protein Variants

EC Number Protein Variants Comment Organism
3.2.1.25 D206N in contrast to the wild-type enzyme which shows a catalytic efficiency for 4-nitrophenyl beta-D-mannopyranoside that is 5fold higher than that for 4-nitrophenyl beta-D-galactopyranoside and 4fold higher than that for 4-nitrophenyl beta-D-glucopyranoside, the mutant enzyme shows highest catalytic efficiency towards 4-nitrophenyl beta-D-glucopyranoside, 11fold higher than that for 4-nitrophenyl beta-D-galactopyranoside and 60fold higher than that for 4-nitrophenyl beta-D-mannopyranoside Pyrococcus horikoshii
3.2.1.25 Q77R in contrast to the wild-type enzyme which shows a catalytic efficiency for 4-nitrophenyl beta-D-mannopyranoside that is 5fold higher than that for 4-nitrophenyl beta-D-galactopyranoside and 4fold higher than that for 4-nitrophenyl beta-D-glucopyranoside, the mutant enzyme shows highest catalytic efficiency towards 4-nitrophenyl beta-D-glucopyranoside, 2fold higher than that for 4-nitrophenyl beta-D-galactopyranoside and 1.1fold higher than that for 4-nitrophenyl beta-D-mannopyranoside Pyrococcus horikoshii
3.2.1.25 Q77R/D206N in contrast to the wild-type enzyme which shows a catalytic efficiency for 4-nitrophenyl beta-D-mannopyranoside that is 5fold higher than that for 4-nitrophenyl beta-D-galactopyranoside and 4fold higher than that for 4-nitrophenyl beta-D-glucopyranoside, the mutant enzyme shows highest catalytic efficiency towards 4-nitrophenyl beta-D-glucopyranoside, 8fold higher than that for 4-nitrophenyl beta-D-galactopyranoside and 1.4fold higher than that for 4-nitrophenyl beta-D-mannopyranoside Pyrococcus horikoshii
3.2.1.B28 N206N about 300fold decrease in catalytic efficiency for 4-nitrophenyl-beta-D-glucospyranoside, about 50fold decrease in catalytic efficiency for 4-nitrophenyl-beta-D-galactoside Pyrococcus furiosus
3.2.1.B28 R77Q 2000fold decrease in catalytic efficiency for 4-nitrophenyl-beta-D-glucospyranoside, 175fold decrease in catalytic efficiency for 4-nitrophenyl-beta-D-galactoside. The mutant enzyme shows a biphasic behavior for the hydrolysis of 4-nitrophenyl beta-D-mannopyranoside with separate kinetic parameters above and below 1 mM 4-nitrophenyl beta-D-mannopyranoside Pyrococcus furiosus
3.2.1.B28 R77Q/N206D about 600fold decrease in catalytic efficiency for 4-nitrophenyl-beta-D-glucospyranoside, about 430fold decrease in catalytic efficiency for 4-nitrophenyl-beta-D-galactoside. The mutant enzyme shows a biphasic behavior for the hydrolysis of 4-nitrophenyl beta-D-mannopyranoside with separate kinetic parameters above and below 1 mM 4-nitrophenyl beta-D-mannopyranoside Pyrococcus furiosus

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.2.1.25 (5R,6R,7S,8S)-5-(hydroxymethyl)-2-phenyl-5,6,7,8-tetrahydroimidazol[1,2-a]pyridine-6,7,8-triol
-
 Pyrococcus horikoshii
3.2.1.B28 (5R,6R,7S,8S)-5-(hydroxymethyl)-2-phenyl-5,6,7,8-tetrahydroimidazol[1,2-a]pyridine-6,7,8-triol
-
 Pyrococcus furiosus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.2.1.25 0.3
-
 4-nitrophenyl beta-D-glucopyranoside pH 5.0, 90°C, mutant enzyme D206N Pyrococcus horikoshii
3.2.1.25 0.44
-
 4-nitrophenyl beta-D-mannopyranoside pH 5.0, 90°C, wild-type enzyme Pyrococcus horikoshii
3.2.1.25 0.68
-
 4-nitrophenyl beta-D-mannopyranoside pH 5.0, 90°C, mutant enzyme Q77R/D206N Pyrococcus horikoshii
3.2.1.25 1.1
-
 4-nitrophenyl beta-D-mannopyranoside pH 5.0, 90°C, mutant enzyme Q77R Pyrococcus horikoshii
3.2.1.25 3.2
-
 4-nitrophenyl beta-D-mannopyranoside pH 5.0, 90°C, mutant enzyme D206N Pyrococcus horikoshii
3.2.1.25 7.3
-
 4-nitrophenyl beta-D-galactopyranoside pH 5.0, 90°C, wild-type enzyme Pyrococcus horikoshii
3.2.1.25 7.8
-
 4-nitrophenyl beta-D-galactopyranoside pH 5.0, 90°C, mutant enzyme D206N Pyrococcus horikoshii
3.2.1.25 13.5
-
 4-nitrophenyl beta-D-glucopyranoside pH 5.0, 90°C, wild-type enzyme Pyrococcus horikoshii
3.2.1.25 16.2
-
 4-nitrophenyl beta-D-glucopyranoside pH 5.0, 90°C, mutant enzyme Q77R Pyrococcus horikoshii
3.2.1.25 16.8
-
 4-nitrophenyl beta-D-galactopyranoside pH 5.0, 90°C, mutant enzyme Q77R Pyrococcus horikoshii
3.2.1.25 30.4
-
 4-nitrophenyl beta-D-glucopyranoside pH 5.0, 90°C, mutant enzyme Q77R/D206N Pyrococcus horikoshii
3.2.1.25 36.1
-
 4-nitrophenyl beta-D-galactopyranoside pH 5.0, 90°C, mutant enzyme Q77R/D206N Pyrococcus horikoshii
3.2.1.B28 additional information
-
 additional information mutants enzymes R77Q and R77Q/N206D show a biphasic behavior for the hydrolysis of 4-nitrophenyl beta-D-mannopyranoside with separate kinetic parameters above and below 1 mM 4-nitrophenyl beta-D-mannopyranoside Pyrococcus furiosus
3.2.1.B28 0.1
-
 4-nitrophenyl beta-D-mannopyranoside pH 5.0, 90°C, mutant enzyme R77Q/N206D, below 1 mM 4-nitrophenyl beta-D-mannopyranoside. The mutant enzyme shows a biphasic behavior for the hydrolysis of 4-nitrophenyl beta-D-mannopyranoside with separate kinetic parameters above and below 1 mM 4-nitrophenyl beta-D-mannopyranoside Pyrococcus furiosus
3.2.1.B28 0.15
-
 4-nitrophenyl beta-D-mannopyranoside pH 5.0, 90°C, mutant enzyme R77Q, below 1 mM 4-nitrophenyl beta-D-mannopyranoside. The mutant enzyme shows a biphasic behavior for the hydrolysis of 4-nitrophenyl beta-D-mannopyranoside with separate kinetic parameters above and below 1 mM 4-nitrophenyl beta-D-mannopyranoside Pyrococcus furiosus
3.2.1.B28 0.19
-
 4-nitrophenyl beta-D-glucopyranoside pH 5.0, 90°C, wild-type enzyme Pyrococcus furiosus
3.2.1.B28 0.63
-
 4-nitrophenyl beta-D-mannopyranoside pH 5.0, 90°C, mutant enzyme N206D Pyrococcus furiosus
3.2.1.B28 0.64
-
 4-nitrophenyl beta-D-mannopyranoside pH 5.0, 90°C, mutant enzyme R77Q, above 1 mM 4-nitrophenyl beta-D-mannopyranoside. The mutant enzyme shows a biphasic behavior for the hydrolysis of 4-nitrophenyl beta-D-mannopyranoside with separate kinetic parameters above and below 1 mM 4-nitrophenyl beta-D-mannopyranoside Pyrococcus furiosus
3.2.1.B28 1.3
-
 4-nitrophenyl beta-D-mannopyranoside pH 5.0, 90°C, wild-type enzyme Pyrococcus furiosus
3.2.1.B28 1.5
-
 4-nitrophenyl beta-D-mannopyranoside pH 5.0, 90°C, mutant enzyme R77Q/N206D, above 1 mM 4-nitrophenyl beta-D-mannopyranoside. The mutant enzyme shows a biphasic behavior for the hydrolysis of 4-nitrophenyl beta-D-mannopyranoside with separate kinetic parameters above and below 1 mM 4-nitrophenyl beta-D-mannopyranoside Pyrococcus furiosus
3.2.1.B28 4.6
-
 4-nitrophenyl beta-D-glucopyranoside pH 5.0, 90°C, mutant enzyme N206D Pyrococcus furiosus
3.2.1.B28 5
-
 4-nitrophenyl beta-D-galactopyranoside pH 5.0, 90°C, wild-type enzyme Pyrococcus furiosus
3.2.1.B28 13.8
-
 4-nitrophenyl beta-D-glucopyranoside pH 5.0, 90°C, mutant enzyme R77Q Pyrococcus furiosus
3.2.1.B28 13.9
-
 4-nitrophenyl beta-D-glucopyranoside pH 5.0, 90°C, mutant enzyme R77Q/N206D Pyrococcus furiosus
3.2.1.B28 15.7
-
 4-nitrophenyl beta-D-galactopyranoside pH 5.0, 90°C, mutant enzyme N206D Pyrococcus furiosus
3.2.1.B28 21.7
-
 4-nitrophenyl beta-D-galactopyranoside pH 5.0, 90°C, mutant enzyme R77Q Pyrococcus furiosus
3.2.1.B28 22
-
 4-nitrophenyl beta-D-galactopyranoside pH 5.0, 90°C, mutant enzyme R77Q/N206D Pyrococcus furiosus

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.2.1.25 56457
-
 4 * 56457, calculated from sequence Pyrococcus horikoshii
3.2.1.25 56500
-
 4 * 56500, SDS-PAGE Pyrococcus horikoshii
3.2.1.25 250000
-
 gel filtration Pyrococcus horikoshii

Organism

EC Number Organism UniProt Comment Textmining
3.2.1.25 Pyrococcus horikoshii O58237
-
-
3.2.1.25 Pyrococcus horikoshii DSM 12428 O58237
-
-
3.2.1.B28 Pyrococcus furiosus Q51723
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.2.1.25
-
 Pyrococcus horikoshii
3.2.1.B28
-
 Pyrococcus furiosus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.2.1.25 4-nitrophenyl beta-D-galactopyranoside + H2O catalytic efficiency (kcat/Km) of the wild-type enzyme for 4-nitrophenyl beta-D-galactopyranoside is 20% compared to catalytic efficiency (kcat/Km) of the wild-type enzyme for 4-nitrophenyl-beta-D-mannopyranoside Pyrococcus horikoshii 4-nitrophenol + beta-D-galactose
-
 ?
3.2.1.25 4-nitrophenyl beta-D-galactopyranoside + H2O catalytic efficiency (kcat/Km) of the wild-type enzyme for 4-nitrophenyl beta-D-galactopyranoside is 20% compared to catalytic efficiency (kcat/Km) of the wild-type enzyme for 4-nitrophenyl-beta-D-mannopyranoside Pyrococcus horikoshii DSM 12428 4-nitrophenol + beta-D-galactose
-
 ?
3.2.1.25 4-nitrophenyl beta-D-glucopyranoside + H2O catalytic efficiency (kcat/Km) of the wild-type enzyme for 4-nitrophenyl beta-D-glucopyranoside is 26% compared to catalytic efficiency (kcat/Km) of the wild-type enzyme for 4-nitrophenyl beta-D-mannopyranoside. The catalytic efficiency (kcat/Km) of the mutant enzymes Q77R, D206N and Q77R/D206N for 4-nitrophenyl beta-D-glucopyranoside is higher then that for 4-nitrophenyl beta-D-galactopyranoside and 4-nitrophenyl-beta-D-mannopyranoside Pyrococcus horikoshii 4-nitrophenol + beta-D-glucose
-
 ?
3.2.1.25 4-nitrophenyl beta-D-glucopyranoside + H2O catalytic efficiency (kcat/Km) of the wild-type enzyme for 4-nitrophenyl beta-D-glucopyranoside is 26% compared to catalytic efficiency (kcat/Km) of the wild-type enzyme for 4-nitrophenyl beta-D-mannopyranoside. The catalytic efficiency (kcat/Km) of the mutant enzymes Q77R, D206N and Q77R/D206N for 4-nitrophenyl beta-D-glucopyranoside is higher then that for 4-nitrophenyl beta-D-galactopyranoside and 4-nitrophenyl-beta-D-mannopyranoside Pyrococcus horikoshii DSM 12428 4-nitrophenol + beta-D-glucose
-
 ?
3.2.1.25 4-nitrophenyl beta-D-mannopyranoside + H2O
-
 Pyrococcus horikoshii 4-nitrophenol + beta-D-mannose
-
 ?
3.2.1.25 4-nitrophenyl beta-D-mannopyranoside + H2O
-
 Pyrococcus horikoshii DSM 12428 4-nitrophenol + beta-D-mannose
-
 ?
3.2.1.B28 4-nitrophenyl beta-D-galactopyranoside + H2O catalytic efficiency (kcat/Km) for 4-nitrophenyl beta-D-galactopyranoside is 7.6% compared to catalytic catalytic efficiency (kcat/Km) for 4-nitrophenyl beta-D-glucopyranoside Pyrococcus furiosus 4-nitrophenol + beta-D-galactose
-
 ?
3.2.1.B28 4-nitrophenyl beta-D-glucopyranoside + H2O
-
 Pyrococcus furiosus 4-nitrophenol + beta-D-glucose
-
 ?
3.2.1.B28 4-nitrophenyl beta-D-mannopyranoside + H2O catalytic efficiency (kcat/Km) for 4-nitrophenyl beta-D-mannopyranoside is 0.7% compared to catalytic catalytic efficiency (kcat/Km) for 4-nitrophenyl beta-D-glucopyranoside Pyrococcus furiosus 4-nitrophenol + beta-D-mannose
-
 ?

Subunits

EC Number Subunits Comment Organism
3.2.1.25 tetramer 4 * 56500, SDS-PAGE Pyrococcus horikoshii
3.2.1.25 tetramer 4 * 56457, calculated from sequence Pyrococcus horikoshii

Synonyms

EC Number Synonyms Comment Organism
3.2.1.25 BglB
-
 Pyrococcus horikoshii
3.2.1.25 PH0501 locus name Pyrococcus horikoshii
3.2.1.B28 CelB
-
 Pyrococcus furiosus

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.2.1.25 101
-
 melting temperature is 100.7°C Pyrococcus horikoshii
3.2.1.25 102
-
 half-life: 27 min Pyrococcus horikoshii
3.2.1.B28 102
-
 half-life: over 10 h Pyrococcus furiosus
3.2.1.B28 106
-
 melting temperature Pyrococcus furiosus

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.2.1.25 1.6
-
 4-nitrophenyl beta-D-mannopyranoside pH 5.0, 90°C, mutant enzyme Q77R Pyrococcus horikoshii
3.2.1.25 4.2
-
 4-nitrophenyl beta-D-mannopyranoside pH 5.0, 90°C, wild-type enzyme Pyrococcus horikoshii
3.2.1.25 6.8
-
 4-nitrophenyl beta-D-mannopyranoside pH 5.0, 90°C, mutant enzyme Q77R/D206N Pyrococcus horikoshii
3.2.1.25 13.5
-
 4-nitrophenyl beta-D-galactopyranoside pH 5.0, 90°C, wild-type enzyme Pyrococcus horikoshii
3.2.1.25 14.2
-
 4-nitrophenyl beta-D-galactopyranoside pH 5.0, 90°C, mutant enzyme Q77R Pyrococcus horikoshii
3.2.1.25 25.5
-
 4-nitrophenyl beta-D-glucopyranoside pH 5.0, 90°C, mutant enzyme Q77R Pyrococcus horikoshii
3.2.1.25 34.4
-
 4-nitrophenyl beta-D-glucopyranoside pH 5.0, 90°C, wild-type enzyme Pyrococcus horikoshii
3.2.1.25 45
-
 4-nitrophenyl beta-D-mannopyranoside pH 5.0, 90°C, mutant enzyme D206N Pyrococcus horikoshii
3.2.1.25 66.5
-
 4-nitrophenyl beta-D-galactopyranoside pH 5.0, 90°C, mutant enzyme Q77R/D206N Pyrococcus horikoshii
3.2.1.25 252
-
 4-nitrophenyl beta-D-glucopyranoside pH 5.0, 90°C, mutant enzyme D206N Pyrococcus horikoshii
3.2.1.25 439
-
 4-nitrophenyl beta-D-glucopyranoside pH 5.0, 90°C, mutant enzyme Q77R/D206N Pyrococcus horikoshii
3.2.1.25 571
-
 4-nitrophenyl beta-D-galactopyranoside pH 5.0, 90°C, mutant enzyme D206N Pyrococcus horikoshii
3.2.1.B28 additional information
-
 additional information mutants enzymes R77Q and R77Q/N206D show a biphasic behavior for the hydrolysis of 4-nitrophenyl beta-D-mannopyranoside with separate kinetic parameters above and below 1 mM 4-nitrophenyl beta-D-mannopyranoside Pyrococcus furiosus
3.2.1.B28 0.85
-
 4-nitrophenyl beta-D-mannopyranoside pH 5.0, 90°C, mutant enzyme R77Q, below 1 mM 4-nitrophenyl beta-D-mannopyranoside. The mutant enzyme shows a biphasic behavior for the hydrolysis of 4-nitrophenyl beta-D-mannopyranoside with separate kinetic parameters above and below 1 mM 4-nitrophenyl beta-D-mannopyranoside Pyrococcus furiosus
3.2.1.B28 1.02
-
 4-nitrophenyl beta-D-mannopyranoside pH 5.0, 90°C, mutant enzyme R77Q/N206D, below 1 mM 4-nitrophenyl beta-D-mannopyranoside. The mutant enzyme shows a biphasic behavior for the hydrolysis of 4-nitrophenyl beta-D-mannopyranoside with separate kinetic parameters above and below 1 mM 4-nitrophenyl beta-D-mannopyranoside Pyrococcus furiosus
3.2.1.B28 1.22
-
 4-nitrophenyl beta-D-mannopyranoside pH 5.0, 90°C, mutant enzyme R77Q, above 1 mM 4-nitrophenyl beta-D-mannopyranoside. The mutant enzyme shows a biphasic behavior for the hydrolysis of 4-nitrophenyl beta-D-mannopyranoside with separate kinetic parameters above and below 1 mM 4-nitrophenyl beta-D-mannopyranoside Pyrococcus furiosus
3.2.1.B28 1.9
-
 4-nitrophenyl beta-D-mannopyranoside pH 5.0, 90°C, mutant enzyme R77Q/N206D, above 1 mM 4-nitrophenyl beta-D-mannopyranoside. The mutant enzyme shows a biphasic behavior for the hydrolysis of 4-nitrophenyl beta-D-mannopyranoside with separate kinetic parameters above and below 1 mM 4-nitrophenyl beta-D-mannopyranoside Pyrococcus furiosus
3.2.1.B28 1.97
-
 4-nitrophenyl beta-D-mannopyranoside pH 5.0, 90°C, mutant enzyme N206D Pyrococcus furiosus
3.2.1.B28 29.2
-
 4-nitrophenyl beta-D-galactopyranoside pH 5.0, 90°C, mutant enzyme R77Q/N206D Pyrococcus furiosus
3.2.1.B28 65.9
-
 4-nitrophenyl beta-D-mannopyranoside pH 5.0, 90°C, wild-type enzyme Pyrococcus furiosus
3.2.1.B28 69.2
-
 4-nitrophenyl beta-D-galactopyranoside pH 5.0, 90°C, mutant enzyme R77Q Pyrococcus furiosus
3.2.1.B28 116
-
 4-nitrophenyl beta-D-glucopyranoside pH 5.0, 90°C, mutant enzyme N206D Pyrococcus furiosus
3.2.1.B28 172
-
 4-nitrophenyl beta-D-glucopyranoside pH 5.0, 90°C, mutant enzyme R77Q/N206D Pyrococcus furiosus
3.2.1.B28 180
-
 4-nitrophenyl beta-D-galactopyranoside pH 5.0, 90°C, mutant enzyme N206D Pyrococcus furiosus
3.2.1.B28 207
-
 4-nitrophenyl beta-D-glucopyranoside pH 5.0, 90°C, mutant enzyme R77Q Pyrococcus furiosus
3.2.1.B28 1140
-
 4-nitrophenyl beta-D-glucopyranoside pH 5.0, 90°C, wild-type enzyme Pyrococcus furiosus
3.2.1.B28 2827
-
 4-nitrophenyl beta-D-galactopyranoside pH 5.0, 90°C, wild-type enzyme Pyrococcus furiosus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.2.1.25 4.75
-
-
 Pyrococcus horikoshii

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
3.2.1.25 0.000014
-
 (5R,6R,7S,8S)-5-(hydroxymethyl)-2-phenyl-5,6,7,8-tetrahydroimidazol[1,2-a]pyridine-6,7,8-triol pH 5.0, 90°C, mutant enzyme D206N Pyrococcus horikoshii
3.2.1.25 0.02
-
 (5R,6R,7S,8S)-5-(hydroxymethyl)-2-phenyl-5,6,7,8-tetrahydroimidazol[1,2-a]pyridine-6,7,8-triol pH 5.0, 90°C, mutant enzyme Q77R/D206N Pyrococcus horikoshii
3.2.1.25 0.1
-
 (5R,6R,7S,8S)-5-(hydroxymethyl)-2-phenyl-5,6,7,8-tetrahydroimidazol[1,2-a]pyridine-6,7,8-triol pH 5.0, 90°C, wild-type enzyme Pyrococcus horikoshii
3.2.1.25 0.11
-
 (5R,6R,7S,8S)-5-(hydroxymethyl)-2-phenyl-5,6,7,8-tetrahydroimidazol[1,2-a]pyridine-6,7,8-triol pH 5.0, 90°C, mutant enzyme Q77R Pyrococcus horikoshii
3.2.1.B28 0.0000065
-
 (5R,6R,7S,8S)-5-(hydroxymethyl)-2-phenyl-5,6,7,8-tetrahydroimidazol[1,2-a]pyridine-6,7,8-triol pH 5.0, 90°C, wild-type enzyme Pyrococcus furiosus
3.2.1.B28 0.000097
-
 (5R,6R,7S,8S)-5-(hydroxymethyl)-2-phenyl-5,6,7,8-tetrahydroimidazol[1,2-a]pyridine-6,7,8-triol pH 5.0, 90°C, mutant enzyme R77Q Pyrococcus furiosus
3.2.1.B28 0.0027
-
 (5R,6R,7S,8S)-5-(hydroxymethyl)-2-phenyl-5,6,7,8-tetrahydroimidazol[1,2-a]pyridine-6,7,8-triol pH 5.0, 90°C, mutant enzyme R77Q/N206D Pyrococcus furiosus
3.2.1.B28 0.0098
-
 (5R,6R,7S,8S)-5-(hydroxymethyl)-2-phenyl-5,6,7,8-tetrahydroimidazol[1,2-a]pyridine-6,7,8-triol pH 5.0, 90°C, mutant enzyme N206D Pyrococcus furiosus

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
3.2.1.25 0.85
-
 4-nitrophenyl beta-D-galactopyranoside pH 5.0, 90°C, mutant enzyme Q77R Pyrococcus horikoshii
3.2.1.25 1.4
-
 4-nitrophenyl beta-D-mannopyranoside pH 5.0, 90°C, mutant enzyme Q77R Pyrococcus horikoshii
3.2.1.25 1.6
-
 4-nitrophenyl beta-D-glucopyranoside pH 5.0, 90°C, mutant enzyme Q77R Pyrococcus horikoshii
3.2.1.25 1.8
-
 4-nitrophenyl beta-D-galactopyranoside pH 5.0, 90°C, mutant enzyme Q77R/D206N Pyrococcus horikoshii
3.2.1.25 1.9
-
 4-nitrophenyl beta-D-galactopyranoside pH 5.0, 90°C, wild-type enzyme Pyrococcus horikoshii
3.2.1.25 2.58
-
 4-nitrophenyl beta-D-glucopyranoside pH 5.0, 90°C, wild-type enzyme Pyrococcus horikoshii
3.2.1.25 9.8
-
 4-nitrophenyl beta-D-mannopyranoside pH 5.0, 90°C, wild-type enzyme Pyrococcus horikoshii
3.2.1.25 9.9
-
 4-nitrophenyl beta-D-mannopyranoside pH 5.0, 90°C, mutant enzyme Q77R/D206N Pyrococcus horikoshii
3.2.1.25 14.4
-
 4-nitrophenyl beta-D-glucopyranoside pH 5.0, 90°C, mutant enzyme Q77R/D206N Pyrococcus horikoshii
3.2.1.25 14.7
-
 4-nitrophenyl beta-D-mannopyranoside pH 5.0, 90°C, mutant enzyme D206N Pyrococcus horikoshii
3.2.1.25 75.8
-
 4-nitrophenyl beta-D-galactopyranoside pH 5.0, 90°C, mutant enzyme D206N Pyrococcus horikoshii
3.2.1.25 870
-
 4-nitrophenyl beta-D-glucopyranoside pH 5.0, 90°C, mutant enzyme D206N Pyrococcus horikoshii
3.2.1.B28 additional information
-
 additional information mutants enzymes R77Q and R77Q/N206D show a biphasic behavior for the hydrolysis of 4-nitrophenyl beta-D-mannopyranoside with separate kinetic parameters above and below 1 mM 4-nitrophenyl beta-D-mannopyranoside Pyrococcus furiosus
3.2.1.B28 1.3
-
 4-nitrophenyl beta-D-galactopyranoside pH 5.0, 90°C, mutant enzyme R77Q/N206D Pyrococcus furiosus
3.2.1.B28 1.3
-
 4-nitrophenyl beta-D-mannopyranoside pH 5.0, 90°C, mutant enzyme R77Q/N206D, above 1 mM 4-nitrophenyl beta-D-mannopyranoside. The mutant enzyme shows a biphasic behavior for the hydrolysis of 4-nitrophenyl beta-D-mannopyranoside with separate kinetic parameters above and below 1 mM 4-nitrophenyl beta-D-mannopyranoside Pyrococcus furiosus
3.2.1.B28 1.9
-
 4-nitrophenyl beta-D-mannopyranoside pH 5.0, 90°C, mutant enzyme R77Q, above 1 mM 4-nitrophenyl beta-D-mannopyranoside. The mutant enzyme shows a biphasic behavior for the hydrolysis of 4-nitrophenyl beta-D-mannopyranoside with separate kinetic parameters above and below 1 mM 4-nitrophenyl beta-D-mannopyranoside Pyrococcus furiosus
3.2.1.B28 3.1
-
 4-nitrophenyl beta-D-mannopyranoside pH 5.0, 90°C, mutant enzyme N206D Pyrococcus furiosus
3.2.1.B28 3.2
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 4-nitrophenyl beta-D-galactopyranoside pH 5.0, 90°C, mutant enzyme R77Q Pyrococcus furiosus
3.2.1.B28 5.7
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 4-nitrophenyl beta-D-mannopyranoside pH 5.0, 90°C, mutant enzyme R77Q, below 1 mM 4-nitrophenyl beta-D-mannopyranoside. The mutant enzyme shows a biphasic behavior for the hydrolysis of 4-nitrophenyl beta-D-mannopyranoside with separate kinetic parameters above and below 1 mM 4-nitrophenyl beta-D-mannopyranoside Pyrococcus furiosus
3.2.1.B28 10.2
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 4-nitrophenyl beta-D-mannopyranoside pH 5.0, 90°C, mutant enzyme R77Q/N206D, below 1 mM 4-nitrophenyl beta-D-mannopyranoside. The mutant enzyme shows a biphasic behavior for the hydrolysis of 4-nitrophenyl beta-D-mannopyranoside with separate kinetic parameters above and below 1 mM 4-nitrophenyl beta-D-mannopyranoside Pyrococcus furiosus
3.2.1.B28 11.5
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 4-nitrophenyl beta-D-galactopyranoside pH 5.0, 90°C, mutant enzyme N206D Pyrococcus furiosus
3.2.1.B28 12.3
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 4-nitrophenyl beta-D-glucopyranoside pH 5.0, 90°C, mutant enzyme R77Q/N206D Pyrococcus furiosus
3.2.1.B28 14.9
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 4-nitrophenyl beta-D-glucopyranoside pH 5.0, 90°C, mutant enzyme R77Q Pyrococcus furiosus
3.2.1.B28 24.9
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 4-nitrophenyl beta-D-glucopyranoside pH 5.0, 90°C, mutant enzyme N206D Pyrococcus furiosus
3.2.1.B28 49.8
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 4-nitrophenyl beta-D-mannopyranoside pH 5.0, 90°C, wild-type enzyme Pyrococcus furiosus
3.2.1.B28 561
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 4-nitrophenyl beta-D-galactopyranoside pH 5.0, 90°C, wild-type enzyme Pyrococcus furiosus
3.2.1.B28 7337
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 4-nitrophenyl beta-D-glucopyranoside pH 5.0, 90°C, wild-type enzyme Pyrococcus furiosus