Information on EC 4.1.2.26 - Phenylserine aldolase:
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EC NUMBERCOMMENTARY
4.1.2.26-

RECOMMENDED NAMEGeneOntology No.
Phenylserine aldolaseGO:0050179

REACTIONREACTION DIAGRAMCOMMENTARYORGANISM UNIPROT ACCESSION NO.LITERATURE
L-threo-3-Phenylserine = glycine + benzaldehyde
show the reaction diagram		----

REACTION TYPEORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
condensation----
elimination--of an aldehyde, C-C bond cleavage-

PATHWAYKEGG LinkMetaCyc Link
No entries in this field

SYSTEMATIC NAMEIUBMB Comments
L-threo-3-phenylserine benzaldehyde-lyase (glycine-forming)A pyridoxal-phosphate protein.

SYNONYMSORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
5-dehydro-2-deoxy-D-gluconate-6-phosphate malonate-semialdehyde-lyase----
Aldolase, phenylserine----

CAS REGISTRY NUMBERCOMMENTARY
37290-60-1-

ORGANISMCOMMENTARYLITERATURESEQUENCE CODESEQUENCE DB SOURCE
Bos tauruscow5111--Manually annotated by BRENDA team
Cavia porcellus-5111--Manually annotated by BRENDA team
Homo sapiens-5111--Manually annotated by BRENDA team
Mus musculus-5111--Manually annotated by BRENDA team
Ovis aries-5111--Manually annotated by BRENDA team
Pseudomonas putidastrain 24-1663708Q59IT3SwissProtManually annotated by BRENDA team
Pseudomonas putida 24. Janstrain 24-1663708Q59IT3SwissProtManually annotated by BRENDA team
Rattus norvegicus-5111--Manually annotated by BRENDA team
Sus scrofa-5111--Manually 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
glycine + benzaldehydeL-threo-3-phenylserine + L-erythro-3-phenylserine
show the reaction diagram		Pseudomonas putidaQ59IT3-663708--r
L-allo-Thrglycine + acetaldehyde
show the reaction diagram		Pseudomonas putidaQ59IT3-663708--?
L-erythro-3-phenylserineglycine + benzaldehyde
show the reaction diagram		Pseudomonas putidaQ59IT3no activity with D-erythro-3-phenylserine663708--r
L-Thrglycine + acetaldehyde
show the reaction diagram		Pseudomonas putidaQ59IT3-663708--?
L-threo-3-phenylserineglycine + benzaldehyde
show the reaction diagram		Ovis aries-r, no activity with D-threo-3-phenylserine5111-5111-
L-threo-3-phenylserineglycine + benzaldehyde
show the reaction diagram		Pseudomonas putidaQ59IT3no activity with D-threo-3-phenylserine663708--r
additional information?-Pseudomonas putidaQ59IT3inducible enzyme663708---
additional information?-Pseudomonas putidaQ59IT3no activity with D-Ser, L-Ser, D-Thr, D-allo-Thr, DL-3-hydroxyphenylethylamine, DL-2-amino-3-phenyl-n-butanoate, L-3-phenyllactate, DL-homoserine, D-glucosaminate, D-mannosamine, D-glucosamine, or D-galactosamine663708---

NATURAL SUBSTRATESNATURAL PRODUCTSREACTION DIAGRAMORGANISM UNIPROT ACCESSION NO.COMMENTARY SUBSTRATELITERATURE
(Substrate)		COMMENTARY PRODUCTLITERATURE
(Product)
additional information?-Pseudomonas putidaQ59IT3inducible enzyme663708--

COFACTORORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATUREIMAGE
pyridoxal 5'-phosphateOvis aries-coenzyme5111 2D-image
pyridoxal 5'-phosphatePseudomonas putidaQ59IT30.7 mol of pyridoxal 5'-phosphate per mol of subunit, K213 of the enzyme probably forms a Schiff base with pyridoxal 5'-phosphate663708 2D-image

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

INHIBITORSORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
3-(ethylamino)phenolPseudomonas putidaQ59IT3competitive against DL-threo-3-phenylserine663708 2D-image
D-cycloserinePseudomonas putidaQ59IT31 mM, 98% inhibition663708 2D-image
DL-3-hydroxy-n-butyratePseudomonas putidaQ59IT320 mM, 30% inhibition663708 2D-image
DL-3-hydroxynorvalinePseudomonas putidaQ59IT320 mM, 49% inhibition663708 2D-image
DL-3-hydroxyphenylethylaminePseudomonas putidaQ59IT320 mM, 79% inhibition663708 2D-image
hydroxylamineOvis aries--5111 2D-image
hydroxylaminePseudomonas putidaQ59IT31 mM, 97% inhibition663708 2D-image
L-3-phenyllactatePseudomonas putidaQ59IT310 mM, 39% inhibition663708 2D-image
p-chloromercuribenzoateOvis aries--5111 2D-image
phenylhydrazinePseudomonas putidaQ59IT31 mM, 52% inhibition663708 2D-image
phosphateOvis aries--5111 2D-image
SemicarbazidePseudomonas putidaQ59IT31 mM, 97% inhibition663708 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
22-L-allo-ThrPseudomonas putidaQ59IT3pH 8.5, 30°C663708 2D-image
4.6-L-erythro-3-phenylserinePseudomonas putidaQ59IT3pH 8.5, 30°C663708 2D-image
29-L-ThrPseudomonas putidaQ59IT3pH 8.5, 30°C663708 2D-image
1.3-L-threo-3-phenylserinePseudomonas putidaQ59IT3pH 8.5, 30°C663708 2D-image

TURNOVER NUMBER [1/s] TURNOVER NUMBER MAXIMUM[1/s] SUBSTRATEORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
1300-L-allo-ThrPseudomonas putidaQ59IT3pH 8.5, 30°C663708 2D-image
7900-L-erythro-3-phenylserinePseudomonas putidaQ59IT3pH 8.5, 30°C663708 2D-image
580-L-ThrPseudomonas putidaQ59IT3pH 8.5, 30°C663708 2D-image
2300-L-threo-3-phenylserinePseudomonas putidaQ59IT3pH 8.5, 30°C663708 2D-image

kcat/KM VALUE [1/mMs-1]kcat/KM VALUE [1/mMs-1] MaximumSUBSTRATEORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
No entries in this field

Ki VALUE [mM]Ki VALUE [mM] MaximumINHIBITORORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
4.1-3-(ethylamino)phenolPseudomonas putidaQ59IT3-663708 2D-image

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
4.3-Pseudomonas putidaQ59IT3reaction with glycine and benzaldehyde663708
300-Pseudomonas putidaQ59IT3cleavage of L-threo-3-phenylserine663708

pH OPTIMUMpH MAXIMUMORGANISM UNIPROT ACCESSION NO. COMMENTARYLITERATURE
7.5-Pseudomonas putidaQ59IT3reaction with glycine and benzyldehyde663708
7.6-Ovis aries--5111
8.5-Pseudomonas putidaQ59IT3reaction with L-threo-3-phenylserine663708

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

TEMPERATURE OPTIMUMTEMPERATURE OPTIMUM MAXIMUMORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
55-Ovis aries--5111

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
kidneyBos taurus, Cavia porcellus, Homo sapiens, Mus musculus, Ovis aries, Rattus norvegicus, Sus scrofa--5111Manually annotated by BRENDA team
liverBos taurus, Cavia porcellus, Homo sapiens, Mus musculus, Ovis aries, Rattus norvegicus, Sus scrofa--5111Manually annotated by BRENDA team
additional informationBos taurus, Cavia porcellus, Homo sapiens, Mus musculus, Ovis aries, Rattus norvegicus, Sus scrofa-not: skeletal muscle, heart muscle, brain spleen, adrenals, red cells, plasma, serum5111Manually annotated by BRENDA team

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

PDBSCOPCATHORGANISM
1v72, downloadSCOP (1v72)CATH (1v72)Pseudomonas putida

MOLECULAR WEIGHT MOLECULAR WEIGHT MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
210000-Pseudomonas putidaQ59IT3gel filtration663708

SUBUNITS ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
hexamerPseudomonas putidaQ59IT36 * 37400, calculation from nucleotide sequence; 6 * 38000, SDS-PAGE663708

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
6.59.5Pseudomonas putidaQ59IT330°C, 10 min, stable663708

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
-20°C, pH 7.2, 10 mM TES buffer, 0.01% 2-mercaptoethanol, 0.05 mM pyridoxal 5'-phosphate, 30% glycerol, stable for several monthsPseudomonas putidaQ59IT3663708

Purification/COMMENTARY ORGANISM UNIPROT ACCESSION NO. LITERATURE
recombinantPseudomonas putidaQ59IT3663708

Cloned/COMMENTARY ORGANISM UNIPROT ACCESSION NO. LITERATURE
overexpression in Escherichia coliPseudomonas putidaQ59IT3663708

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

ENGINEERINGORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
K213QPseudomonas putidaQ59IT3loss of activity, disappearance of absorption maximum at 420 nm663708

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

APPLICATIONORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
No entries in this field

DISEASETITLE OF PUBLICATIONLINK TO PUBMED
No entries in this field

REF. AUTHORS TITLE JOURNAL VOL. PAGES YEAR ORGANISMLINK TO PUBMEDSOURCE
5111Bruns, F.H.; Fiedler, L.Enzymatic cleavage and synthesis of L-threo-beta-phenylserine and L-erythro-beta-phenylserineNature1811533-15341958Bos taurus, Cavia porcellus, Homo sapiens, Mus musculus, Ovis aries, Rattus norvegicus, Sus scrofa PubMed
663708Misono, H.; Maeda, H.; Tuda, K.; Ueshima, S.; Miyazaki, N.; Nagata, S.Characterization of an inducible phenylserine aldolase from Pseudomonas putida 24-1Appl. Environ. Microbiol.714602-46092005Pseudomonas putida PubMed

LINKS TO OTHER DATABASES (specific for EC-Number 4.1.2.26)
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)