2.4.1.230: kojibiose phosphorylase
This is an abbreviated version!
For detailed information about kojibiose phosphorylase, go to the full flat file.
Word Map on EC 2.4.1.230
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2.4.1.230
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brockii
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thermoanaerobacter
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maltose
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phosphorylases
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phosphorolysis
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proteinase
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saccharide
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trehalose
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oligosaccharides
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keratinolytic
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1-phosphate
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corneum
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glycoside
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pepstatin
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albicans
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stratum
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trisaccharide
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nigerose
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synthesis
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saccharolyticus
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chymostatin
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2d-nmr
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l-sorbose
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dermatophytosis
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beta-d-glucose
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canis
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scalp
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caldicellulosiruptor
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hsqc-tocsy
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microsporum
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brevis
- 2.4.1.230
- brockii
-
thermoanaerobacter
- maltose
- phosphorylases
-
phosphorolysis
- proteinase
-
saccharide
- trehalose
- oligosaccharides
-
keratinolytic
- 1-phosphate
- corneum
- glycoside
- pepstatin
- albicans
-
stratum
- trisaccharide
- nigerose
- synthesis
- saccharolyticus
- chymostatin
-
2d-nmr
- l-sorbose
- dermatophytosis
- beta-d-glucose
- canis
-
scalp
-
caldicellulosiruptor
-
hsqc-tocsy
- microsporum
- brevis
Reaction
Synonyms
CsKP, kojibiose phosphorylase, KPase, PsKP, Py04_1502, YcjT
ECTree
2.4.1.230 kojibiose phosphorylaseAdvanced search results
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results (Engineering
Engineering on EC 2.4.1.230 - kojibiose phosphorylase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
E392R
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
E392R/T417A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
E392R/T417I
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
T417A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
T417F
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
T417I
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
W391M/E392V
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
W391M/E392V/T417A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
W391M/E392V/T417I
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
D459N
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increase in Km-values for kojibiose, beta-D-glucose 1-phosphate and glucose
additional information
additional information
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substitution of maltose phosphorylase, EC 2.4.1.8, His413-Glu421, His413-Ile418 and His413-Glu415 from loop 3, that include His413 and Glu415 presumably recognising the alpha-anomeric O-1 group of the glucose moiety at subsite 1+, by corresponding to segments from Ser426-Ala431 in trehalose phosphorylase, EC 2.4.1.64, and Thr419-Phe427 in kojibiose phosphorylase, EC 2.4.1.230, thus confers the maltose phosphorylase with phosphorolytic activity towards trehalose and kojibiose, respectively
additional information
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substitution of maltose phosphorylase, EC 2.4.1.8, His413-Glu421, His413-Ile418 and His413-Glu415 from loop 3, that include His413 and Glu415 presumably recognising the alpha-anomeric O-1 group of the glucose moiety at subsite 1+, by corresponding to segments from Ser426-Ala431 in trehalose phosphorylase, EC 2.4.1.64, and Thr419-Phe427 in kojibiose phosphorylase, EC 2.4.1.230, thus confers the maltose phosphorylase with phosphorolytic activity towards trehalose and kojibiose, respectively
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additional information
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chimeric phosphorylases are constructed of the kojibiose phosphorylase gene and the trehalose phosphorylase gene from Thermoanaerobacter brockii. Chimera V-III show not trehalose phosphorylase, but kojibiose phosphorylase activity, although only 125 amino acid residues in 785 residues of chimera VIII are from that of kojibiose phosphorylase. Chimera V-III have 1% of the specific activity of the wild-type kojibiose phosphorylase. The temperature profile and kinetic parameters of chimera V-III are remarkably changed as compared to those of the wild-type kojibiose phosphorylase. Chimera VIII protein exists as a monomer in solution, whereas wild-type kojibiose phosphorylase and trehalose phosphorylase are hexamer and dimer structures, respectively. The chimera acts on nigerose, sophorose and laminaribiose, in addition to kojibiose. Chimera VIII is also able to act on sophorose and laminaribiose in the absence of inorganic phosphate, and produces two trisaccharides, beta-D-glucosyl-(1,6)-laminaribiose and laminaritriose, from laminaribiose
