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Information on EC 2.4.1.216 - trehalose 6-phosphate phosphorylase and Organism(s) Lactococcus lactis and UniProt Accession Q9CID5

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EC Tree
     2 Transferases
         2.4 Glycosyltransferases
             2.4.1 Hexosyltransferases
                2.4.1.216 trehalose 6-phosphate phosphorylase
IUBMB Comments
The enzyme from Lactococcus lactis is specific for trehalose 6-phosphate. Differs from EC 2.4.1.64, alpha,alpha-trehalose phosphorylase, in that trehalose is not a substrate.
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This record set is specific for:
Lactococcus lactis
UNIPROT: Q9CID5
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Word Map
The taxonomic range for the selected organisms is: Lactococcus lactis
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
trepp, trehalose 6-phosphate phosphorylase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Phosphorylation
-
-
-
-
glycosyl group transfer
-
-
-
-
phospho group transfer
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-
SYSTEMATIC NAME
IUBMB Comments
alpha,alpha-trehalose 6-phosphate:phosphate beta-D-glucosyltransferase
The enzyme from Lactococcus lactis is specific for trehalose 6-phosphate. Differs from EC 2.4.1.64, alpha,alpha-trehalose phosphorylase, in that trehalose is not a substrate.
CAS REGISTRY NUMBER
COMMENTARY hide
403512-51-6
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
trehalose 6-phosphate + phosphate
glucose 6-phosphate + beta-D-glucose 1-phosphate
show the reaction diagram
formation of trehalose 6-phosphate is favoured
-
r
trehalose 6-phosphate + phosphate
glucose 6-phosphate + beta-D-glucose 1-phosphate
show the reaction diagram
-
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
trehalose 6-phosphate + phosphate
glucose 6-phosphate + beta-D-glucose 1-phosphate
show the reaction diagram
formation of trehalose 6-phosphate is favoured
-
r
trehalose 6-phosphate + phosphate
glucose 6-phosphate + beta-D-glucose 1-phosphate
show the reaction diagram
-
-
-
?
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.9
beta-D-glucose 1-phosphate
-
4
glucose 6-phosphate
-
6
trehalose 6-phosphate
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7
-
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
-
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
CAA77100
SwissProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
-
genes trePP and pgmB, encoding trehalose 6-phosphate phosphorylase and beta-phosphoglucomutase, respectively, enable the synthesis of trehalose 6-phosphate in the organism
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
94000
gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
1 * 94000, SDS-PAGE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
endogenous genes trePP and pgmB, encoding trehalose 6-phosphate phosphorylase and beta-phosphoglucomutase, respectively, provide the synthesis of trehalose 6-phosphate, which can be transformed into trehalose by transgenically expressed trehalose 6-phosphate phosphatase, the respective gene otsB from the food-grade organism Propionibacterium freudenreichii is expressed in Lactobacillus lactis. Trehalose-producing strains show improved tolerance of 5 to 10fold higher survivability to acid at pH 3.0 and cold shock of 4°C, also a strong improvement in cell survival in response to heat shock of 45°C is achieved, but no protection is rendered against dehydration, phenotype overview
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
overexpression in Escherichia coli and Lactococcus lactis
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Andersson U.; Radstrm, P.
beta-Glucose 1-phosphate-interconverting enzymes in maltose- and trehalose-fermenting lactic acid bacteria
Environ. Microbiol.
4
81-88
2002
Carnobacterium divergens, Carnobacterium maltaromaticum, Carnobacterium sp., Carnobacterium sp. 496, Enterococcus faecalis, Enterococcus faecium, Lactiplantibacillus pentosus, Lactiplantibacillus plantarum, Lactobacillus casei ssp. casei, Lactobacillus delbrueckii ssp. delbrueckii, Lactococcus lactis, Lactococcus lactis ssp. cremoris, Lactococcus lactis ssp. lactis, Lactococcus plantarum, Lactococcus raffinolactis, Leuconostoc mesenteroides ssp. dextranicum, Leuconostoc pseudomesenteroides, Leuconostoc weissella, Limosilactobacillus reuteri, Oenococcus oeni, Pediococcus acidilactici, Pediococcus damnosus, Pediococcus pentosaceus, Tetragenococcus halophilus, Vagococcus salmoninarum, Weissella viridescens
Manually annotated by BRENDA team
Andersson, U.; Levander, F.; Radstrm, P.
Trehalose-6-phosphate phosphorylase is part of a novel metabolic pathway for trehalose utilization in Lactococcus lactis
J. Biol. Chem.
276
42707-42713
2001
Lactococcus lactis (Q9CID5), Lactococcus lactis, Lactococcus lactis IL1403 (Q9CID5)
Manually annotated by BRENDA team
Carvalho, A.L.; Cardoso, F.S.; Bohn, A.; Neves, A.R.; Santos, H.
Engineering trehalose synthesis in Lactococcus lactis for improved stress tolerance
Appl. Environ. Microbiol.
77
4189-4199
2011
Lactococcus lactis, Lactococcus lactis MG1363
Manually annotated by BRENDA team