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Literature summary extracted from

  • Yeom, S.J.; Seo, E.S.; Kim, Y.S.; Oh, D.K.
    Increased D-allose production by the R132E mutant of ribose-5-phosphate isomerase from Clostridium thermocellum (2011), Appl. Microbiol. Biotechnol., 89, 1859-1866.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
5.3.1.6 expressed in Escherichia coli ER2566 cells Acetivibrio thermocellus

Protein Variants

EC Number Protein Variants Comment Organism
5.3.1.6 C65A the mutant shows no activity for D-psicose Acetivibrio thermocellus
5.3.1.6 D8A the mutant shows no activity for D-psicose Acetivibrio thermocellus
5.3.1.6 H133A the mutant shows 15% activity compared to the wild type enzyme Acetivibrio thermocellus
5.3.1.6 H98A the mutant shows 13% activity compared to the wild type enzyme Acetivibrio thermocellus
5.3.1.6 H9A the mutant shows 63% activity compared to the wild type enzyme Acetivibrio thermocellus
5.3.1.6 N99A the mutant shows 35% activity compared to the wild type enzyme Acetivibrio thermocellus
5.3.1.6 R132A the mutant exhibits an increase in D-psicose isomerization activity (116% activity compared to the wild type enzyme) Acetivibrio thermocellus
5.3.1.6 R132D the mutant shows increased catalytic efficiency toward D-psicose compared to the wild type enzyme Acetivibrio thermocellus
5.3.1.6 R132E the mutant shows increased catalytic efficiency toward D-psicose compared to the wild type enzyme Acetivibrio thermocellus
5.3.1.6 R132E the specific activity and catalytic efficiency (kcat/Km) of the R132E mutant for D-psicose are 1.4 and 1.5fold higher than those of the wild type enzyme, respectively Acetivibrio thermocellus
5.3.1.6 R132I the mutant shows decreased catalytic efficiency toward D-psicose compared to the wild type enzyme Acetivibrio thermocellus
5.3.1.6 R132K the mutant shows decreased catalytic efficiency toward D-psicose compared to the wild type enzyme Acetivibrio thermocellus
5.3.1.6 R132Q the mutant shows decreased catalytic efficiency toward D-psicose compared to the wild type enzyme Acetivibrio thermocellus
5.3.1.6 R136A the mutant shows 15% activity compared to the wild type enzyme Acetivibrio thermocellus
5.3.1.6 T135A the mutant shows 91% activity compared to the wild type enzyme Acetivibrio thermocellus
5.3.1.6 T67A the mutant shows 46% activity compared to the wild type enzyme Acetivibrio thermocellus
5.3.1.6 Y42A the mutant shows no activity for D-psicose Acetivibrio thermocellus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
5.3.1.6 43
-
 D-psicose mutant enzyme R132E, pH 7.5, 80°C Acetivibrio thermocellus
5.3.1.6 46
-
 D-psicose mutant enzyme R132D, pH 7.5, 80°C Acetivibrio thermocellus
5.3.1.6 53
-
 D-psicose mutant enzyme R132K, pH 7.5, 80°C Acetivibrio thermocellus
5.3.1.6 53
-
 D-psicose wild type enzyme, pH 7.5, 80°C Acetivibrio thermocellus
5.3.1.6 54
-
 D-psicose mutant enzyme R132Q, pH 7.5, 80°C Acetivibrio thermocellus
5.3.1.6 56
-
 D-psicose mutant enzyme R132A, pH 7.5, 80°C Acetivibrio thermocellus
5.3.1.6 78
-
 D-psicose mutant enzyme R132I, pH 7.5, 80°C Acetivibrio thermocellus

Organism

EC Number Organism UniProt Comment Textmining
5.3.1.6 Acetivibrio thermocellus A3DIL8
-
-
5.3.1.6 Acetivibrio thermocellus ATCC 27405 A3DIL8
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
5.3.1.6 HisTrap HP column chromatography Acetivibrio thermocellus

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
5.3.1.6 0.259
-
 mutant enzyme H98A, using D-psicose as substrate, pH 7.5, 80°C Acetivibrio thermocellus
5.3.1.6 0.299
-
 mutant enzyme H133A, using D-psicose as substrate, pH 7.5, 80°C Acetivibrio thermocellus
5.3.1.6 0.299
-
 mutant enzyme R136A, using D-psicose as substrate, pH 7.5, 80°C Acetivibrio thermocellus
5.3.1.6 0.698
-
 mutant enzyme N99A, using D-psicose as substrate, pH 7.5, 80°C Acetivibrio thermocellus
5.3.1.6 0.917
-
 mutant enzyme T67A, using D-psicose as substrate, pH 7.5, 80°C Acetivibrio thermocellus
5.3.1.6 1.256
-
 mutant enzyme H9A, using D-psicose as substrate, pH 7.5, 80°C Acetivibrio thermocellus
5.3.1.6 1.815
-
 mutant enzyme T135A, using D-psicose as substrate, pH 7.5, 80°C Acetivibrio thermocellus
5.3.1.6 1.994
-
 wild type enzyme, using D-psicose as substrate, pH 7.5, 80°C Acetivibrio thermocellus
5.3.1.6 2.313
-
 mutant enzyme R132A, using D-psicose as substrate, pH 7.5, 80°C Acetivibrio thermocellus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
5.3.1.6 D-psicose the conversion yield of D-psicose to D-allose is 32% for the R132E mutant enzyme and 25% for the wild type enzyme after 80 min Acetivibrio thermocellus D-allose
-
 r
5.3.1.6 D-psicose the conversion yield of D-psicose to D-allose is 32% for the R132E mutant enzyme and 25% for the wild type enzyme after 80 min Acetivibrio thermocellus ATCC 27405 D-allose
-
 r
5.3.1.6 D-ribulose 5-phosphate
-
 Acetivibrio thermocellus D-ribose 5-phosphate
-
 r
5.3.1.6 D-ribulose 5-phosphate
-
 Acetivibrio thermocellus ATCC 27405 D-ribose 5-phosphate
-
 r

Synonyms

EC Number Synonyms Comment Organism
5.3.1.6 CTRpiB
-
 Acetivibrio thermocellus
5.3.1.6 ribose-5-phosphate isomerase
-
 Acetivibrio thermocellus

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
5.3.1.6 80
-
-
 Acetivibrio thermocellus

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
5.3.1.6 60 90
-
 Acetivibrio thermocellus

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
5.3.1.6 60 75 the half-lives of the wild type enzyme at 60°C, 65°C, 70°C, 75°C, and 80°C are 11, 7.0, 4.2, 1.5, and 0.6 h, respectively Acetivibrio thermocellus

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
5.3.1.6 1962
-
 D-psicose mutant enzyme R132K, pH 7.5, 80°C Acetivibrio thermocellus
5.3.1.6 2211
-
 D-psicose mutant enzyme R132I, pH 7.5, 80°C Acetivibrio thermocellus
5.3.1.6 2335
-
 D-psicose mutant enzyme R132Q, pH 7.5, 80°C Acetivibrio thermocellus
5.3.1.6 2347
-
 D-psicose wild type enzyme, pH 7.5, 80°C Acetivibrio thermocellus
5.3.1.6 2580
-
 D-psicose mutant enzyme R132A, pH 7.5, 80°C Acetivibrio thermocellus
5.3.1.6 2674
-
 D-psicose mutant enzyme R132D, pH 7.5, 80°C Acetivibrio thermocellus
5.3.1.6 2743
-
 D-psicose mutant enzyme R132E, pH 7.5, 80°C Acetivibrio thermocellus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
5.3.1.6 7.5
-
-
 Acetivibrio thermocellus

pH Range

EC Number pH Minimum pH Maximum Comment Organism
5.3.1.6 6 9
-
 Acetivibrio thermocellus

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
5.3.1.6 28
-
 D-psicose mutant enzyme R132I, pH 7.5, 80°C Acetivibrio thermocellus
5.3.1.6 37
-
 D-psicose mutant enzyme R132K, pH 7.5, 80°C Acetivibrio thermocellus
5.3.1.6 43
-
 D-psicose mutant enzyme R132Q, pH 7.5, 80°C Acetivibrio thermocellus
5.3.1.6 44
-
 D-psicose wild type enzyme, pH 7.5, 80°C Acetivibrio thermocellus
5.3.1.6 46
-
 D-psicose mutant enzyme R132A, pH 7.5, 80°C Acetivibrio thermocellus
5.3.1.6 58
-
 D-psicose mutant enzyme R132D, pH 7.5, 80°C Acetivibrio thermocellus
5.3.1.6 64
-
 D-psicose mutant enzyme R132E, pH 7.5, 80°C Acetivibrio thermocellus