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Information on EC 4.1.2.49 - L-allo-threonine aldolase and Organism(s) Aeromonas jandaei and UniProt Accession O07051
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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.
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Word Map
- 4.1.2.49
- aeromonas
- l-threonine
- pyridoxal
- jandaei
-
stereoselective
-
schiff
- 5'-phosphate
-
low-specific
The taxonomic range for the selected organisms is: Aeromonas jandaei
The expected taxonomic range for this enzyme is: Bacteria, Archaea
The expected taxonomic range for this enzyme is: Bacteria, Archaea
Synonyms
l-allo-threonine aldolase, l-allo-ta, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
PATHWAY SOURCE
PATHWAYS
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.
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-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-beta-phenylserine + H2O
glycine + benzaldehyde
Vmax/KM is 33% compared to DL-threo-3,4-dihydroxyphenylserine
-
-
?
additional information
?
-
no activity with L-threonine or L-serine
-
-
?
L-allo-threonine
glycine + acetaldehyde
Vmax/KM is 97% compared to DL-threo-3,4-dihydroxyphenylserine
-
-
?
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
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
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
tetramer
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
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
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
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
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
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