Any feedback?
Information on EC 4.1.2.49 - L-allo-threonine aldolase
for references in articles please use BRENDA:EC4.1.2.49Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
4.1.2.49 L-allo-threonine aldolaseIUBMB Comments
Requires pyridoxal phosphate. This enzyme, characterized from the bacterium Aeromonas jandaei, is specific for L-allo-threonine and can not act on either L-threonine or L-serine. Different from EC 4.1.2.5, L-threonine aldolase, and EC 4.1.2.48, low-specificity L-threonine aldolase. A previously listed enzyme with this name, EC 4.1.2.6, was deleted in 1971 after it was found to be identical to EC 2.1.2.1, glycine hydroxymethyltransferase.
Specify your search results
Word Map
- 4.1.2.49
- aeromonas
- l-threonine
- pyridoxal
- jandaei
-
stereoselective
-
schiff
- 5'-phosphate
-
low-specific
The expected taxonomic range for this enzyme is: Bacteria, Archaea
Synonyms
l-allo-threonine aldolase, l-allo-ta, 
more
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
L-allo-TA
L-allo-threonine acetaldehyde-lyase
LATA
ltaA
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-allo-threonine = glycine + acetaldehyde
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PATHWAY SOURCE
PATHWAYS
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYSTEMATIC NAME
IUBMB Comments
L-allo-threonine acetaldehyde-lyase (glycine-forming)
Requires pyridoxal phosphate. This enzyme, characterized from the bacterium Aeromonas jandaei, is specific for L-allo-threonine and can not act on either L-threonine or L-serine. Different from EC 4.1.2.5, L-threonine aldolase, and EC 4.1.2.48, low-specificity L-threonine aldolase. A previously listed enzyme with this name, EC 4.1.2.6, was deleted in 1971 after it was found to be identical to EC 2.1.2.1, glycine hydroxymethyltransferase.
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
DL-threo-beta-phenylserine + H2O
glycine + benzaldehyde
Vmax/KM is 33% compared to DL-threo-3,4-dihydroxyphenylserine
-
-
?
DL-beta-hydroxynorvaline + H2O
glycine + propionaldehyde
Vmax/KM is 4% compared to DL-threo-3,4-dihydroxyphenylserine
-
-
?
DL-beta-hydroxynorvaline + H2O
glycine + propionaldehyde
Vmax/KM is 4% compared to DL-threo-3,4-dihydroxyphenylserine
-
-
?
DL-threo-3,4-dihydroxyphenylserine + H2O
glycine + 3,4-dihydroxybenzaldehyde
-
-
-
?
DL-threo-3,4-dihydroxyphenylserine + H2O
glycine + 3,4-dihydroxybenzaldehyde
-
-
-
?
L-allo-threonine
glycine + acetaldehyde
Vmax/KM is 97% compared to DL-threo-3,4-dihydroxyphenylserine
-
-
?
L-allo-threonine
glycine + acetaldehyde
Vmax/KM is 97% compared to DL-threo-3,4-dihydroxyphenylserine
-
-
?
additional information
?
-
no activity with L-threonine or L-serine
-
-
?
additional information
?
-
no activity with L-threonine or L-serine
-
-
?
additional information
?
-
-
no activity with L-threonine or L-serine
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL 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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pyridoxal 5'-phosphate
Lys199 probably functions as an essential catalytic residue forming an internal Schiff base with pyridoxal 5'-phosphate of the enzyme to catalyze the reversible aldol reaction
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
27.8
DL-beta-hydroxynorvaline
pH 7.4, temperature not specified in the publication
6.77
DL-threo-3,4-Dihydroxyphenylserine
pH 7.4, temperature not specified in the publication
19.6
DL-threo-beta-phenylserine
pH 7.4, temperature not specified in the publication
1.45
L-allo-threonine
pH 7.4, temperature not specified in the publication
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
208
DL-threo-beta-phenylserine, pH 7.4, temperature not specified in the publication
217
DL-threo-3,4-dihydroxyphenylserine, pH 7.4, temperature not specified in the publication
37.1
DL-beta-hydroxynorvaline, pH 7.4, temperature not specified in the publication
45.2
L-allo-threonine, pH 7.4, temperature not specified in the publication
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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.
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Show AA Sequence and Transmembrane Helices (397 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PDB
SCOP
CATH
UNIPROT
ORGANISM
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.
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
tetramer
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
sitting-drop vapour-diffusion method, crystal structures of wild-type enzyme and its mutant H128Y/S292R are determined at 2.59 and 2.50 A resolution
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D168N
mutation reduces the specific activity, which is partially restored by the addition of excess pyridoxal 5'-phosphate to the reaction mixture. The mutant enzyme is able to catalyse the aldol synthesis of L-beta-phenylserine from benzaldehyde and glycine with yields similar to the wild-type enzyme
D168S
mutation reduces the specific activity, which is partially restored by the addition of excess pyridoxal 5'-phosphate to the reaction mixture. The mutant enzyme is able to catalyse the aldol synthesis of L-beta-phenylserine from benzaldehyde and glycine with yields similar to the wild-type enzyme
D168T
mutation reduces the specific activity, which is partially restored by the addition of excess pyridoxal 5'-phosphate to the reaction mixture. The mutant enzyme is able to catalyse the aldol synthesis of L-beta-phenylserine from benzaldehyde and glycine with yields similar to the wild-type enzyme
D168V
mutation reduces the specific activity, which is partially restored by the addition of excess pyridoxal 5'-phosphate to the reaction mixture. The mutant enzyme is able to catalyse the aldol synthesis of L-beta-phenylserine from benzaldehyde and glycine with yields similar to the wild-type enzyme
H128Y
8.4fold increase in activity towards L-threonine and a 2.0fold increase towards L-allo-threonine compared with the wild-type enzyme
H128Y/S292R
3fold and 322fold increased kcat/Km values towards towards L-allo-threonine and L-threonine compared with the wild-type enzyme
K199R
mutation reduces the specific activity of the enzyme by 5000fold, which can be partially restored by adding an excess of pyridoxal 5'-phosphate to the reaction medium
K224A
mutant enzyme shows properties similar to the wild type enzyme
R171F
loss of specific activity by more than 2000fold. pyridoxal 5'-phosphate-glycine complex is not obtained for the mutant. The mutant is not active in the aldol condensation reaction to produce L-beta-phenylserine
R231A
the mutant enzyme racemizes L-alanine to D-alanine, whereas the wild-type enzyme is not active towards L-alanine
R313H
catalytic activity of the mutant in the retro-aldol cleavage of L-allo-threonine is decreased by 200fold mainly due to increase in Km. Mutation hinders the formation of the quinonoid complex to stabilize the carbanion after initial bond cleavage. L-beta-Phenylserine product in the aldol condensation is obtained with the conversion rate similar to the wild-type enzyme
H128Y
-
8.4fold increase in activity towards L-threonine and a 2.0fold increase towards L-allo-threonine compared with the wild-type enzyme
-
H128Y/S292R
-
3fold and 322fold increased kcat/Km values towards towards L-allo-threonine and L-threonine compared with the wild-type enzyme
-
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kataoka, M.; Wada, M.; Nishi, K.; Yamada, H.; Shimizu, S.
Purification and characterization of L-allo-threonine aldolase from Aeromonas jandaei DK-39
FEMS Microbiol. Lett.
151
245-248
1997
Aeromonas jandaei (O07051), Aeromonas jandaei DK-39 (O07051), Aeromonas jandaei DK-39
brenda
Liu, J.Q.; Dairi, T.; Kataoka, M.; Shimizu, S.; Yamada, H.
L-allo-Threonine aldolase from Aeromonas jandaei DK-39: gene cloning, nucleotide sequencing, and identification of the pyridoxal 5'-phosphate-binding lysine residue by site-directed mutagenesis
J. Bacteriol.
179
3555-3560
1997
Aeromonas jandaei (O07051), Aeromonas jandaei DK-39 (O07051), Aeromonas jandaei DK-39
brenda
Qin, H.M.; Imai, F.L.; Miyakawa, T.; Kataoka, M.; Kitamura, N.; Urano, N.; Mori, K.; Kawabata, H.; Okai, M.; Ohtsuka, J.; Hou, F.; Nagata, K.; Shimizu, S.; Tanokura, M.
L-allo-threonine aldolase with an H128Y/S292R mutation from Aeromonas jandaei DK-39 reveals the structural basis of changes in substrate stereoselectivity
Acta Crystallogr. Sect. D
70
1695-1703
2014
Aeromonas jandaei (O07051), Aeromonas jandaei DK-39 (O07051), Aeromonas jandaei DK-39
brenda
Fesko, K.; Suplatov, D.; Svedas, V.
Bioinformatic analysis of the fold type I PLP-dependent enzymes reveals determinants of reaction specificity in L-threonine aldolase from Aeromonas jandaei
FEBS open bio
8
1013-1028
2018
Aeromonas jandaei (O07051)
brenda
Select items on the left to see more content.
EXTERNAL LINKS (specific for EC-Number 4.1.2.49)
html completed
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
About BRENDA
Social media
Help
Survey
Download
Contribution
Legal
Curated at
Member of
