Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 2.2.1.2 - transaldolase and Organism(s) Saccharomyces cerevisiae and UniProt Accession P15019

for references in articles please use BRENDA:EC2.2.1.2
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
     2 Transferases
         2.2 Transferring aldehyde or ketonic groups
             2.2.1 Transketolases and transaldolases
                2.2.1.2 transaldolase
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Saccharomyces cerevisiae
UNIPROT: P15019 not found.
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
The taxonomic range for the selected organisms is: Saccharomyces cerevisiae
The enzyme appears in selected viruses and cellular organisms
Synonyms
transaldolase, taldo1, dihydroxyacetone synthase, taldo, transaldolase 1, transaldolase b, fotal, transaldolase a, talase, peroxisomal transaldolase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dihydroxyacetone synthase
-
-
-
-
dihydroxyacetonetransferase
-
-
-
-
formaldehyde transketolase
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate = D-erythrose 4-phosphate + D-fructose 6-phosphate
show the reaction diagram
mechanism
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
aldehyde group transfer
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
sedoheptulose-7-phosphate:D-glyceraldehyde-3-phosphate glyceronetransferase
-
CAS REGISTRY NUMBER
COMMENTARY hide
9014-46-4
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2,5-D-threo-diketohexose phosphate + D-glyceraldehyde 3-phosphate
?
show the reaction diagram
-
-
-
-
?
D-erythrose + sedoheptulose 7-phosphate
?
show the reaction diagram
-
-
-
-
?
D-erythrose 4-phosphate + sedoheptulose 7-phosphate
?
show the reaction diagram
-
-
-
-
?
D-fructose 6-phosphate + D-glyceraldehyde 3-phosphate
?
show the reaction diagram
-
-
-
-
?
D-fructose 6-phosphate + erythrose 4-phosphate
sedoheptulose 7-phosphate + glyceraldehyde 3-phosphate
show the reaction diagram
D-glyceraldehyde + sedoheptulose 7-phosphate
?
show the reaction diagram
-
-
-
-
?
D-ribose 5-phosphate + sedoheptulose 7-phosphate
?
show the reaction diagram
-
-
-
-
?
hydroxypyruvic aldehyde + sedoheptulose 7-phosphate
?
show the reaction diagram
-
-
-
-
?
L-glyceraldehyde 3-phosphate + sedoheptulose 7-phosphate
?
show the reaction diagram
-
-
-
-
?
L-sorbose 6-phosphate + D-glyceraldehyde 3-phosphate
?
show the reaction diagram
-
-
-
-
?
octulose 8-phosphate + D-glyceraldehyde 3-phosphate
?
show the reaction diagram
-
-
-
-
?
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
D-erythrose 4-phosphate + D-fructose 6-phosphate
show the reaction diagram
sedoheptulose phosphate + D-glyceraldehyde 3-phosphate
?
show the reaction diagram
-
-
-
-
?
additional information
?
-
-
enzyme participates in the interconversion of metabolically significant triose, tetrose, pentose, hexose and heptose phosphates, enzyme is involved in the metabolism of carbohydrates via the nonoxidative part of the pentose phosphate pathway
-
-
?
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
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
D-erythrose 4-phosphate + D-fructose 6-phosphate
show the reaction diagram
-
-
-
-
r
additional information
?
-
-
enzyme participates in the interconversion of metabolically significant triose, tetrose, pentose, hexose and heptose phosphates, enzyme is involved in the metabolism of carbohydrates via the nonoxidative part of the pentose phosphate pathway
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
no cofactor requirement
-
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.018
D-erythrose 4-phosphate
-
-
0.32
D-fructose 6-phosphate
-
-
0.22
glyceraldehyde 3-phosphate
-
-
0.18
sedoheptulose 7-phosphate
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
gene disruption mutant displays a significant decrease in both growth on xylose and xylose-fermenting ability
malfunction
dysfunction could lead to liver cirrhosis and neonatal multi-organ diseases
physiological function
key enzyme in pentose phosphate pathway
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging-drop vapor diffusion method
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Ni2+ affinity column
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli BL21
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
expression of is up-regulated in the presence of xylose
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Tsolas, O.; Horecker, B.L.
Transaldolase
The Enzymes, 3rd Ed. (Boyer, P. D. , ed. )
7
259-280
1972
Bos taurus, Saccharomyces cerevisiae, Cyberlindnera jadinii, Chlorella sp., Prosthecochloris vibrioformis f. thiosulfatophilum, Chromatium sp., Oryctolagus cuniculus, Escherichia coli, Euglena sp., Homo sapiens, Musca domestica, Rattus norvegicus, Saccharomyces pastorianus, Spinacia oleracea, Tetranychus telarius
-
Manually annotated by BRENDA team
Huang, H.; Rong, H.; Li, X.; Tong, S.; Zhu, Z.; Niu, L.; Teng, M.
The crystal structure and identification of NQM1/YGRO43C, a transaldolase from Saccharomyces cerevisiae
Proteins Struct. Funct. Genet.
73
1076-1081
2008
Saccharomyces cerevisiae (P53228), Saccharomyces cerevisiae
Manually annotated by BRENDA team
Matsushika, A.; Goshima, T.; Fujii, T.; Inoue, H.; Sawayama, S.; Yano, S.
Characterization of non-oxidative transaldolase and transketolase enzymes in the pentose phosphate pathway with regard to xylose utilization by recombinant Saccharomyces cerevisiae
Enzyme Microb. Technol.
51
16-25
2012
Saccharomyces cerevisiae (P15019), Saccharomyces cerevisiae
Manually annotated by BRENDA team