Information on EC 4.1.2.49 - L-allo-threonine aldolase:
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EC NUMBERCOMMENTARY
4.1.2.49-

RECOMMENDED NAMEGeneOntology No.
L-allo-threonine aldolase-

REACTIONREACTION DIAGRAMCOMMENTARYORGANISM UNIPROT ACCESSION NO.LITERATURE
L-allo-threonine = glycine + acetaldehyde
show the reaction diagram		----

REACTION TYPEORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
No entries in this field

PATHWAYKEGG LinkMetaCyc Link
No entries in this field

SYSTEMATIC NAMEIUBMB 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.

SYNONYMSORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
L-allo-TAAeromonas jandaei--715334
L-allo-threonine acetaldehyde-lyaseAeromonas jandaei--715045

CAS REGISTRY NUMBERCOMMENTARY
No entries in this field

ORGANISMCOMMENTARYLITERATURESEQUENCE CODESEQUENCE DB SOURCE
Aeromonas jandaei-715045, 715334O07051UniProtManually annotated by BRENDA team
Aeromonas jandaei DK-39-715045O07051SwissProtManually annotated by BRENDA team

GENERAL INFORMATIONORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
No entries in this field

SUBSTRATEPRODUCT                      REACTION DIAGRAMORGANISM UNIPROT ACCESSION NO. COMMENTARY/
Substrate		 LITERATURE/
Substrate		 COMMENTARY/
Product		 LITERATURE/
Product		 Reversibility
r=reversible
ir=irreversible
?=not specified
DL-beta-hydroxynorvaline + H2Oglycine + propionaldehyde
show the reaction diagram		Aeromonas jandaeiO07051Vmax/KM is 4% compared to DL-threo-3,4-dihydroxyphenylserine715045--?
DL-threo-3,4-dihydroxyphenylserine + H2Oglycine + 3,4-dihydroxybenzaldehyde
show the reaction diagram		Aeromonas jandaeiO07051-715045--?
DL-threo-beta-phenylserine + H2Oglycine + benzaldehyde
show the reaction diagram		Aeromonas jandaeiO07051Vmax/KM is 33% compared to DL-threo-3,4-dihydroxyphenylserine715045--?
L-allo-threonineglycine + acetaldehyde
show the reaction diagram		Aeromonas jandaeiO07051-715045--?
L-allo-threonineglycine + acetaldehyde
show the reaction diagram		Aeromonas jandaei--715334--r
L-allo-threonineglycine + acetaldehyde
show the reaction diagram		Aeromonas jandaeiO07051Vmax/KM is 97% compared to DL-threo-3,4-dihydroxyphenylserine715045--?
additional information?-Aeromonas jandaeiO07051no activity with L-threonine or L-serine715045---

NATURAL SUBSTRATESNATURAL PRODUCTSREACTION DIAGRAMORGANISM UNIPROT ACCESSION NO.COMMENTARY SUBSTRATELITERATURE
(Substrate)		COMMENTARY PRODUCTLITERATURE
(Product)
L-allo-threonineglycine + acetaldehyde
show the reaction diagram		Aeromonas jandaeiO07051-715045--

COFACTORORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATUREIMAGE
pyridoxal 5'-phosphateAeromonas jandaei-required715045 2D-image
pyridoxal 5'-phosphateAeromonas jandaei-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 reaction715334 2D-image

METALS and IONS ORGANISM UNIPROT ACCESSION NO.COMMENTARY LITERATURE
No entries in this field

INHIBITORSORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
4-chloromercuribenzoateAeromonas jandaei-1 mM, 76% inhibition715045 2D-image
5,5'-dithiobis(2-nitrobenzoic acid)Aeromonas jandaei-1 mM, 100% inhibition715045 2D-image
AcriflavineAeromonas jandaei-1 mM, 65% inhibition715045 2D-image
Ag2SO4Aeromonas jandaei-1 mM, 100% inhibition715045 2D-image
AlCl3Aeromonas jandaei-1 mM, 69% inhibition715045 2D-image
CdCl2Aeromonas jandaei-1 mM, 80% inhibition715045 2D-image
D-(-)-penicillamineAeromonas jandaei-1 mM, 87% inhibition715045 2D-image
FeCl3Aeromonas jandaei-1 mM, 100% inhibition715045 2D-image
FeSO4Aeromonas jandaei-1 mM, 100% inhibition715045 2D-image
HgCl2Aeromonas jandaei-1 mM, 99% inhibition715045 2D-image
hydroxylamineAeromonas jandaei-1 mM, 100% inhibition715045 2D-image
iodoacetamideAeromonas jandaei-1 mM, 56% inhibition715045 2D-image
N-bromosuccinimideAeromonas jandaei-1 mM, 89% inhibition715045 2D-image
phenylhydrazineAeromonas jandaei-1 mM, 91% inhibition715045 2D-image
SemicarbazideAeromonas jandaei-1 mM, 63% inhibition715045 2D-image
ZnSO4Aeromonas jandaei-1 mM, 98% inhibition715045 2D-image

ACTIVATING COMPOUNDORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
No entries in this field

KM VALUE [mM]KM VALUE [mM] MaximumSUBSTRATEORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
27.8-DL-beta-hydroxynorvalineAeromonas jandaei-pH 7.4, temperature not specified in the publication715045-
6.77-DL-threo-3,4-DihydroxyphenylserineAeromonas jandaei-pH 7.4, temperature not specified in the publication715045 2D-image
19.6-DL-threo-beta-phenylserineAeromonas jandaei-pH 7.4, temperature not specified in the publication715045 2D-image
0.36-L-allo-threonineAeromonas jandaei-pH 8.0, 30°C, mutant enzyme K51A715334 2D-image
0.37-L-allo-threonineAeromonas jandaei-pH 8.0, 30°C, wild-type enzyme715334 2D-image
0.38-L-allo-threonineAeromonas jandaei-pH 8.0, 30°C, mutant enzyme K224A715334 2D-image
1.45-L-allo-threonineAeromonas jandaei-pH 7.4, temperature not specified in the publication715045 2D-image

TURNOVER NUMBER [1/s] TURNOVER NUMBER MAXIMUM[1/s] SUBSTRATEORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
2.9-L-allo-threonineAeromonas jandaei-pH 8.0, 30°C, mutant enzyme K51A715334 2D-image
3-L-allo-threonineAeromonas jandaei-pH 8.0, 30°C, mutant enzyme K224A; pH 8.0, 30°C, wild-type enzyme715334 2D-image

kcat/KM VALUE [1/mMs-1]kcat/KM VALUE [1/mMs-1] MaximumSUBSTRATEORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
7.9-L-allo-threonineAeromonas jandaei-pH 8.0, 30°C, mutant enzyme K224A71533412053
8.1-L-allo-threonineAeromonas jandaei-pH 8.0, 30°C, mutant enzyme K51A; pH 8.0, 30°C, wild-type enzyme71533412053

Ki VALUE [mM]Ki VALUE [mM] MaximumINHIBITORORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
No entries in this field

IC50 VALUE [mM]IC50 VALUE [mM] MaximumINHIBITORORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
No entries in this field

SPECIFIC ACTIVITY [µmol/min/mg] SPECIFIC ACTIVITY MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
8.4-Aeromonas jandaei-pH 8.0, 30°C715334
37.1-Aeromonas jandaei-DL-beta-hydroxynorvaline, pH 7.4, temperature not specified in the publication715045
45.2-Aeromonas jandaei-L-allo-threonine, pH 7.4, temperature not specified in the publication715045
208-Aeromonas jandaei-DL-threo-beta-phenylserine, pH 7.4, temperature not specified in the publication715045
217-Aeromonas jandaei-DL-threo-3,4-dihydroxyphenylserine, pH 7.4, temperature not specified in the publication715045

pH OPTIMUMpH MAXIMUMORGANISM UNIPROT ACCESSION NO. COMMENTARYLITERATURE
7.4-Aeromonas jandaei-assay at715045
8-Aeromonas jandaei-assay at715334

pH RANGEpH RANGE MAXIMUMORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
No entries in this field

TEMPERATURE OPTIMUMTEMPERATURE OPTIMUM MAXIMUMORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
30-Aeromonas jandaei-assay at715334

TEMPERATURE RANGE TEMPERATURE MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
No entries in this field

pI VALUEpI VALUE MAXIMUMORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
No entries in this field

SOURCE TISSUE ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE SOURCE
No entries in this field

LOCALIZATION ORGANISM UNIPROT ACCESSION NO. COMMENTARY GeneOntology No. LITERATURE SOURCE
No entries in this field

PDBSCOPCATHORGANISM
No entries in this field

MOLECULAR WEIGHT MOLECULAR WEIGHT MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
160000-Aeromonas jandaei-gel filtration715045

SUBUNITS ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
tetramerAeromonas jandaei-4 * 38000, SDS-PAGE715045
tetramerAeromonas jandaei-4 * 36294, calculated from sequence715334

POSTTRANSLATIONAL MODIFICATION ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
No entries in this field

Crystallization/COMMENTARY ORGANISM UNIPROT ACCESSION NO. LITERATURE
No entries in this field

pH STABILITYpH STABILITY MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
No entries in this field

TEMPERATURE STABILITYTEMPERATURE STABILITY MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARYLITERATURE
No entries in this field

GENERAL STABILITYORGANISM UNIPROT ACCESSION NO.LITERATURE
No entries in this field

ORGANIC SOLVENT ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
No entries in this field

OXIDATION STABILITY ORGANISM UNIPROT ACCESSION NO. LITERATURE
No entries in this field

STORAGE STABILITY ORGANISM UNIPROT ACCESSION NO. LITERATURE
No entries in this field

Purification/COMMENTARY ORGANISM UNIPROT ACCESSION NO. LITERATURE
-Aeromonas jandaeiO07051715045, 715334

Cloned/COMMENTARY ORGANISM UNIPROT ACCESSION NO. LITERATURE
overexpressed in recombinant Escherichia coli cellsAeromonas jandaei-715334

EXPRESSION ORGANISM UNIPROT ACCESSION NO. LITERATURE
No entries in this field

ENGINEERINGORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
K199AAeromonas jandaei-catalytically inactive mutant enzyme715334
K224AAeromonas jandaei-mutant enzyme shows properties similar to the wild type enzyme715334
K51AAeromonas jandaei-mutant enzyme shows properties similar to the wild type enzyme715334

Renatured/COMMENTARYORGANISM UNIPROT ACCESSION NO.LITERATURE
No entries in this field

APPLICATIONORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
No entries in this field

REF. AUTHORS TITLE JOURNAL VOL. PAGES YEAR ORGANISMLINK TO PUBMEDSOURCE
715045Kataoka, M.; Wada, M.; Nishi, K.; Yamada, H.; Shimizu, S.Purification and characterization of L-allo-threonine aldolase from Aeromonas jandaei DK-39FEMS Microbiol. Lett.151245-2481997Aeromonas jandaei PubMed
715334Liu, 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 mutagenesisJ. Bacteriol.1793555-35601997Aeromonas jandaei PubMed

LINKS TO OTHER DATABASES (specific for EC-Number 4.1.2.49)
ExplorEnz
ExPASy
KEGG
MetaCyc
NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM
IUBMB Enzyme Nomenclature
PROSITE Database of protein families and domains
SYSTERS
Protein Mutant Database
InterPro (database of protein families, domains and functional sites)