HOME
login
history
all enzymes
BRENDA home
History
Enzyme Nomenclature
Information on EC 2.2.1.8 - fluorothreonine transaldolase
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
The expected taxonomic range for this enzyme is: Streptomyces cattleya
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
EC NUMBER 
COMMENTARY 
2.2.1.8
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
RECOMMENDED NAME
GeneOntology No.
fluorothreonine transaldolase
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
L-threonine + fluoroacetaldehyde = acetaldehyde + 4-fluoro-L-threonine
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
aldehyde group transfer
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYSTEMATIC NAME
IUBMB Comments
fluoroacetaldehyde:L-threonine aldehydetransferase
A pyridoxal phosphate protein. Can also convert chloroacetaldehyde into4-chloro-L-threonine. Unlike EC 2.1.2.1, glycine hydroxymethyltransferase, does not use glycine as a substrate.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CAS REGISTRY NUMBER
COMMENTARY
403503-13-9
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
physiological function
final step of 4-fluorothreonine biosynthesis
physiological function
gene disruption of the transaldolase results in a mutant which can produce fluoroacetate but is blocked in its ability to biosynthesise 4-fluorothreonine, revealing a branchpoint role for the PLP-transaldolase
physiological function
-
gene disruption of the transaldolase results in a mutant which can produce fluoroacetate but is blocked in its ability to biosynthesise 4-fluorothreonine, revealing a branchpoint role for the PLP-transaldolase
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
L-threonine + fluoroacetaldehyde
4-fluoro-L-threonine + acetaldehyde
-
-
-
?
fluoroacetaldehyde + L-threonine
acetaldehyde + 4-fluoro-L-threonine
-
-
-
?
fluoroacetaldehyde + L-threonine
acetaldehyde + 4-fluoro-L-threonine
-
-
-
?
L-threonine + chloroacetaldehyde
acetaldehyde + 4-chloro-L-threonine
-
-
-
?
L-threonine + chloroacetaldehyde
acetaldehyde + 4-chloro-L-threonine
-
-
-
?
L-threonine + fluoroacetaldehyde
acetaldehyde + 4-fluoro-L-threonine
-
C3 and C4 of threonine are replaced with the aldehyde carbons, generating a new molecule of threonine
-
?
L-threonine + fluoroacetaldehyde
acetaldehyde + 4-fluoro-L-threonine
-
the enzyme-PLP complex accepts acetaldehyde as a substrate and generates a new molecule of threonine in a neutral crossover reaction
-
?
L-threonine + fluoroacetaldehyde
acetaldehyde + 4-fluoro-L-threonine
-
enzyme is important in biosynthesis of 4-fluorothreonine
-
-
-
L-threonine + fluoroacetaldehyde
acetaldehyde + 4-fluoro-L-threonine
-
enzyme is important in biosynthesis of 4-fluorothreonine
-
?
L-threonine + fluoroacetaldehyde
acetaldehyde + 4-fluoro-L-threonine
-
C3 and C4 of threonine are replaced with the aldehyde carbons, generating a new molecule of threonine
-
?
L-threonine + fluoroacetaldehyde
acetaldehyde + 4-fluoro-L-threonine
-
enzyme is important in biosynthesis of 4-fluorothreonine
-
?
L-threonine + fluoroacetaldehyde
acetaldehyde + 4-fluoro-L-threonine
-
the enzyme-PLP complex accepts acetaldehyde as a substrate and generates a new molecule of threonine in a neutral crossover reaction
-
?
L-threonine + fluoroacetaldehyde
acetaldehyde + 4-fluoro-L-threonine
-
enzyme is important in biosynthesis of 4-fluorothreonine
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
L-threonine + fluoroacetaldehyde
4-fluoro-L-threonine + acetaldehyde
B6VP39
-
-
-
?
L-threonine + fluoroacetaldehyde
acetaldehyde + 4-fluoro-L-threonine
-
enzyme is important in biosynthesis of 4-fluorothreonine
-
-
-
L-threonine + fluoroacetaldehyde
acetaldehyde + 4-fluoro-L-threonine
-
enzyme is important in biosynthesis of 4-fluorothreonine
-
?
L-threonine + fluoroacetaldehyde
acetaldehyde + 4-fluoro-L-threonine
-
enzyme is important in biosynthesis of 4-fluorothreonine
-
?
L-threonine + fluoroacetaldehyde
acetaldehyde + 4-fluoro-L-threonine
-
enzyme is important in biosynthesis of 4-fluorothreonine
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli BL21, transfection to Streptococcus lividans TK24
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
LINKS TO OTHER DATABASES (specific for EC-Number 2.2.1.8)
html completed
Use of this online version of BRENDA is free for academic research only. Commercial use or download access requires a license. See terms of use.
Information
