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Literature summary for 3.2.1.B26 extracted from

  • Cobucci-Ponzano, B.; Moracci, M.; Lauro, B.; Ciaramella, M.; DAvino, R.; Rossi, M.
    Ionic network at the C-terminus of the beta-glycosidase from the hyperthermophilic archaeon Sulfolobus solfataricus: Functional role in the quaternary structure thermal stabilization (2002), Proteins, 48, 98-106.
    View publication on PubMed
Search for more literature for 3.2.1.B26

Protein Variants

Protein Variants Comment Organism
delHis489 mutation produces faster enzyme inactivation, kcat/KM for 2-nitrophenyl beta-D-galactopyranoside is 45% of the wild-type value Saccharolobus solfataricus
delVal484-His489 clone DELTA6 lacks the last six amino acids (-Val-Lys-Pro-Leu-Arg-His-COOH) and has no additional mutations. Mutation produces faster enzyme inactivation, kcat/KM for 2-nitrophenyl beta-D-galactopyranoside is 37% of the wild-type value Saccharolobus solfataricus
H489A mutation produces faster enzyme inactivation, kcat/KM for 2-nitrophenyl beta-D-galactopyranoside is 85% of the wild-type value Saccharolobus solfataricus
R488A mutation produces faster enzyme inactivation, kcat/KM for 2-nitrophenyl beta-D-galactopyranoside is 90% of the wild-type value Saccharolobus solfataricus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.95
-
 2-nitrophenyl beta-D-galactopyranoside pH 6.5, 65°C, mutant enzyme R488A Saccharolobus solfataricus
0.99
-
 2-nitrophenyl beta-D-galactopyranoside pH 6.5, 65°C, wild-type enzyme Saccharolobus solfataricus
1.47
-
 2-nitrophenyl beta-D-galactopyranoside pH 6.5, 65°C, mutant enzyme R489A Saccharolobus solfataricus
1.9
-
 2-nitrophenyl beta-D-galactopyranoside pH 6.5, 65°C, mutant enzyme His489 Saccharolobus solfataricus
1.97
-
 2-nitrophenyl beta-D-galactopyranoside pH 6.5, 65°C, mutant enzyme delVal484-His489 Saccharolobus solfataricus

Organism

Organism UniProt Comment Textmining
Saccharolobus solfataricus
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2-nitrophenyl beta-D-galactopyranoside + H2O
-
 Saccharolobus solfataricus 2-nitrophenol + beta-D-galactopyranose
-
 ?

Synonyms

Synonyms Comment Organism
SsbetaGly
-
 Saccharolobus solfataricus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
65
-
 assay at Saccharolobus solfataricus

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
additional information
-
 the thermostable enzyme is an interesting model system for the study of protein adaptation to high temperatures. The largest ion-pair network of the enzyme is located at the tetrameric interface of the molecule Saccharolobus solfataricus
85
-
 k(inact): 0.0000061 (wild-type enzyme), 0.00012 (mutant enzyme R488A), 0.00029 (mutant enzyme H489A), 0.00001 (mutant enzyme delHis489) Saccharolobus solfataricus

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
366
-
 2-nitrophenyl beta-D-galactopyranoside pH 6.5, 65°C, mutant enzyme delVal484-His489 Saccharolobus solfataricus
416
-
 2-nitrophenyl beta-D-galactopyranoside pH 6.5, 65°C, mutant enzyme His489 Saccharolobus solfataricus
427
-
 2-nitrophenyl beta-D-galactopyranoside pH 6.5, 65°C, mutant enzyme R488A Saccharolobus solfataricus
498
-
 2-nitrophenyl beta-D-galactopyranoside pH 6.5, 65°C, wild-type enzyme Saccharolobus solfataricus
611
-
 2-nitrophenyl beta-D-galactopyranoside pH 6.5, 65°C, mutant enzyme R489A Saccharolobus solfataricus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6.5
-
 assay at Saccharolobus solfataricus