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Information on EC 4.1.2.5 - L-threonine aldolase

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EC Tree
     4 Lyases
         4.1 Carbon-carbon lyases
             4.1.2 Aldehyde-lyases
                4.1.2.5 L-threonine aldolase
IUBMB Comments
A pyridoxal-phosphate protein. This enzyme is specific for L-threonine and can not utilize L-allo-threonine. Different from EC 4.1.2.49, L-allo-threonine aldolase, and EC 4.1.2.48, low-specificity L-threonine aldolase.
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This record set is specific for:
UNIPROT: Q9X266
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Word Map
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
l-threonine aldolase, l-threonine acetaldehyde-lyase, more
PATHWAY SOURCE
PATHWAYS
-
-, -
SYSTEMATIC NAME
IUBMB Comments
L-threonine acetaldehyde-lyase (glycine-forming)
A pyridoxal-phosphate protein. This enzyme is specific for L-threonine and can not utilize L-allo-threonine. Different from EC 4.1.2.49, L-allo-threonine aldolase, and EC 4.1.2.48, low-specificity L-threonine aldolase.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
glycine + acetaldehyde
L-threonine
show the reaction diagram
-
-
-
r
L-threonine
glycine + acetaldehyde
show the reaction diagram
-
-
-
r
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pyridoxal 5'-phosphate
dependent on
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
Q9X266_THEMA
Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8)
343
0
37574
TrEMBL
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
tetramer
4 * 37000, SDS-PAGE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A21C
L-threonine cleavage activity is similar to the activity of the wild-type enzyme
F85Y
L-threonine cleavage activity is about 65% of the activity of the wild-type enzyme
I124D
L-threonine cleavage activity is about 65% of the activity of the wild-type enzyme
P56C
L-threonine cleavage activity is about 95% of the activity of the wild-type enzyme, the mutant enzyme displays significantly enhanced stability compared to the wild type enzyme
Q22K
L-threonine cleavage activity is about 75% of the activity of the wild-type enzyme
S198D
L-threonine cleavage activity is about 110% of the activity of the wild-type enzyme
T59D
L-threonine cleavage activity is about 10% of the activity of the wild-type enzyme
V235C
L-threonine cleavage activity is about 110% of the activity of the wild-type enzyme
V29D
L-threonine cleavage activity is about 90% of the activity of the wild-type enzyme
W86E
the mutant enzyme displays enhanced activity, with stability similar to the wild type enzyme
additional information
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
75
15 h, 50% loss of activity
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
the gene of L-threonine aldolase from Thermotoga maritima is cloned into c-LEctas expression vector pLE1A17 under control of the T7 promoter. Expression in Escherichia coli BL21(DE3)
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
synthesis
threonine aldolase is a very promising enzyme that can be used to prepare biologically active compounds or building blocks for pharmaceutical industry. Rational design is applied to thermophilic threonine aldolase from Thermotoga maritima to improve thermal stability by the incorporation of salt and disulfide bridges between subunits in the functional tetramer
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Wieteska, L.; Ionov, M.; Szemraj, J.; Feller, C.; Kolinski, A.; Gront, D.
Improving thermal stability of thermophilic L-threonine aldolase from Thermotoga maritima
J. Biotechnol.
199
69-76
2015
Thermotoga maritima (Q9X266), Thermotoga maritima
Manually annotated by BRENDA team