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Information on EC 2.4.1.64 - alpha,alpha-trehalose phosphorylase and Organism(s) Thermoanaerobacter brockii and UniProt Accession Q8L164

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EC Tree
     2 Transferases
         2.4 Glycosyltransferases
             2.4.1 Hexosyltransferases
                2.4.1.64 alpha,alpha-trehalose phosphorylase
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This record set is specific for:
Thermoanaerobacter brockii
UNIPROT: Q8L164 not found.
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Word Map
The taxonomic range for the selected organisms is: Thermoanaerobacter brockii
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
trehalose phosphorylase, bsel_1207, alpha,alpha-trehalose phosphorylase, inverting trehalose phosphorylase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
trehalose phosphorylase
-
phosphorylase, trehalose
-
-
-
-
trehalose phosphorylase
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hexosyl group transfer
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
alpha,alpha-trehalose:phosphate beta-D-glucosyltransferase
-
CAS REGISTRY NUMBER
COMMENTARY hide
37205-59-7
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
beta-D-glucose 1-phosphate + D-galactose
? + phosphate
show the reaction diagram
low activity. The Km value for D-galactose is about 30fold higher than that for D-glucose
-
-
r
D-glucose + beta-D-glucose 1-phosphate
alpha,alpha-trehalose + phosphate
show the reaction diagram
best substrate combination
-
-
r
alpha,alpha-trehalose + phosphate
D-glucose + beta-D-glucose 1-phosphate
show the reaction diagram
beta-D-glucose-1-phosphate + gentiobiose
6-O-beta-D-glucopyranosyl trehalose + phosphate
show the reaction diagram
-
-
-
-
?
beta-D-glucose-1-phosphate + isomaltose
6-O-alpha-D-glucopyranosyl trehalose + phosphate
show the reaction diagram
-
-
-
-
?
beta-D-glucose-1-phosphate + isomaltotriose
?
show the reaction diagram
-
-
-
-
?
beta-D-glucose-1-phosphate + isopanose
?
show the reaction diagram
-
-
-
-
?
beta-D-glucose-1-phosphate + melibiose
6-O-alpha-D-galactopyranosyl trehalose + phosphate
show the reaction diagram
-
-
-
-
?
additional information
?
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3 - 447.6
D-galactose
0.6 - 36.8
D-glucose
0.75
beta-D-glucose 1-phosphate
-
-
0.57
phosphate
-
-
0.97
trehalose
-
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
14 - 66.5
D-galactose
7 - 53.9
D-glucose
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.149 - 1.29
D-galactose
0.872 - 36
D-glucose
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 7
-
synthesis of trehalose
7 - 7.5
-
phosphorolysis of trehalose
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
70
-
both directions
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
previously known as Thermoanaerobium brockii
UniProt
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
TREP_THEBR
774
0
89252
Swiss-Prot
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
190000
-
gel filtration
88000
-
x * 88000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 88000, SDS-PAGE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A431T
the mutant shows strongly decreased catalytic efficiency for D-glucose and decreased catalytic efficiency for D-galactose compared to the wild type enzyme
A440E
the mutant shows increased catalytic efficiency for D-glucose and wild type catalytic efficiency for D-galactose compared to the wild type enzyme
A440K
the mutant shows increased catalytic efficiencies for D-glucose and D-galactose compared to the wild type enzyme
A440M
the mutant shows increased catalytic efficiencies for D-glucose and D-galactose compared to the wild type enzyme
A440V
the mutant shows increased catalytic efficiencies for D-glucose and D-galactose compared to the wild type enzyme
A440V/N657Y
the mutant shows increased catalytic efficiencies for D-glucose and D-galactose compared to the wild type enzyme
A440V/R448S
the mutant shows increased catalytic efficiency for D-glucose and strongly increased catalytic efficiency for D-galactose compared to the wild type enzyme
N657D
the mutant shows increased catalytic efficiencies for D-glucose and D-galactose compared to the wild type enzyme
N657G
the mutant shows increased catalytic efficiencies for D-glucose and D-galactose compared to the wild type enzyme
N657I
the mutant shows approximate 2fold increase in affinity for D-galactose
N657L
the mutant shows increased catalytic efficiencies for D-glucose and D-galactose compared to the wild type enzyme
N657R
the mutant shows increased catalytic efficiencies for D-glucose and D-galactose compared to the wild type enzyme
N657Y
the mutant shows approximate 2fold increase in affinity for D-galactose
P588H
the mutant shows increased catalytic efficiencies for D-glucose and D-galactose compared to the wild type enzyme
R448D
the mutant shows increased catalytic efficiencies for D-glucose and D-galactose compared to the wild type enzyme
R448F
the mutant shows increased catalytic efficiencies for D-glucose and D-galactose compared to the wild type enzyme
R448N
the mutant shows increased catalytic efficiencies for D-glucose and D-galactose compared to the wild type enzyme
R448S
the mutant shows increased catalytic efficiencies for D-glucose and D-galactose compared to the wild type enzyme
R448S/N657Y
the mutant shows about wild type catalytic efficiencies for D-glucose and D-galactose
R448V
the mutant shows increased catalytic efficiencies for D-glucose and D-galactose compared to the wild type enzyme
additional information
-
construction of chimeric phosphorylases of the kojibiose phosphorylase gene and the trehalose phosphorylase gene from Thermoanaerobacter brockii
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 9
-
stable
489328
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
60
the half-life of the wild type enzyme remains constant for about 13 h at 60°C
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Maruta, K.; Mukai, K.; Yamashita, H.; Kubota, M.; Chaen, H.; Fukuda, S.; Kurimoto, M.
Gene encoding a trehalose phosphorylase from Thermoanaerobacter brockii ATCC 35047
Biosci. Biotechnol. Biochem.
66
1976-1980
2002
Thermoanaerobacter brockii
Manually annotated by BRENDA team
Chaen, H.; Nakada, T.; Nishimoto, T.; Kuroda, N.; Fukuda, S.; Sugimoto, T.; Kurimoto, M.; Tsujisaka, Y.
Purification and characterization of thermostable trehalose phosphorylase from Thermoanaerobium brockii
J. Appl. Glycosci.
46
399-405
1999
Thermoanaerobacter brockii
-
Manually annotated by BRENDA team
Yamamoto, T.; Yamashita, H.; Mukai, K.; Watanabe, H.; Kubota, M.; Chaen, H.; Fukuda, S.
Construction and characterization of chimeric enzymes of kojibiose phosphorylase and trehalose phosphorylase from Thermoanaerobacter brockii
Carbohydr. Res.
341
2350-2359
2006
Thermoanaerobacter brockii
Manually annotated by BRENDA team
Maruta, K.; Watanabe, H.; Nishimoto, T.; Kubota, M.; Chaen, H.; Fukuda, S.; Kurimoto, M.; Tsujisaka, Y.
Acceptor specificity of trehalose phosphorylase from Thermoanaerobacter brockii: production of novel nonreducing trisaccharide, 6-O-alpha-D-galactopyranosyl trehalose
J. Biosci. Bioeng.
101
385-390
2006
Thermoanaerobacter brockii
Manually annotated by BRENDA team
Van der Borght, J.; Desmet, T.; Soetaert, W.
Enzymatic production of beta-D-glucose-1-phosphate from trehalose
Biotechnol. J.
5
986-993
2010
Thermoanaerobacter brockii
Manually annotated by BRENDA team
Van der Borght, J.; Soetaert, W.; Desmet, T.
Engineering the acceptor specificity of trehalose phosphorylase for the production of trehalose analogs
Biotechnol. Prog.
28
1257-1262
2012
Thermoanaerobacter brockii (Q8L164), Thermoanaerobacter brockii
Manually annotated by BRENDA team