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Information on EC 2.7.1.35 - pyridoxal kinase and Organism(s) Escherichia coli and UniProt Accession P40191

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IUBMB Comments
Pyridoxine, pyridoxamine and various derivatives can also act as acceptors.
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This record set is specific for:
Escherichia coli
UNIPROT: P40191
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The taxonomic range for the selected organisms is: Escherichia coli
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
pyridoxal kinase, pyridoxine kinase, pl kinase, ldpdxk, pyridoxal phosphokinase, stplk, epl kinase 1, pn kinase, hpl kinase, epl kinase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ePL kinase 1
-
pyridoxal kinase 1
-
ePL kinase
-
two different forms encoded by genes PdxK and PdxY yielding kinase 1 and kinase 2, low activity of kinase 2 suggests that this kinase originally has another substrate but can also utilize pyridoxal
kinase (phosphorylating), pyridoxal
-
-
-
-
kinase, pyridoxal (phosphorylating)
-
-
-
-
PL kinase
-
-
-
-
PLK
-
-
-
-
PM kinase
-
-
-
-
PN kinase
-
-
-
-
PN/PL/PM kinase
-
-
-
-
pyridoxal 5-phosphate-kinase
-
-
-
-
pyridoxal kinase
-
-
-
-
pyridoxal kinase-like protein SOS4
-
-
-
-
pyridoxal phosphokinase
-
-
-
-
pyridoxamine kinase
-
-
-
-
pyridoxine kinase
-
-
-
-
pyridoxine/pyridoxal/pyridoxamine kinase
-
-
-
-
vitamin B6 kinase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phospho group transfer
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -, -
SYSTEMATIC NAME
IUBMB Comments
ATP:pyridoxal 5'-phosphotransferase
Pyridoxine, pyridoxamine and various derivatives can also act as acceptors.
CAS REGISTRY NUMBER
COMMENTARY hide
9026-42-0
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + pyridoxine
ADP + pyridoxine 5'-phosphate
show the reaction diagram
-
-
-
?
ATP + pyridoxal
ADP + pyridoxal 5'-phosphate
show the reaction diagram
ATP + pyridoxamine
ADP + pyridoxamine 5'-phosphate
show the reaction diagram
-
-
-
-
?
ATP + pyridoxine
ADP + pyridoxine 5'-phosphate
show the reaction diagram
-
-
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + pyridoxal
ADP + pyridoxal 5'-phosphate
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
K+
in the absence of any potassium ion, the activity is less than 5% of the maximum activity
Zn2+
-
in complex with ATP preferred substrate in vitro
additional information
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pyridoxal
-
-
pyridoxal 5'-phosphate
-
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.07 - 0.6
ATP
0.1 - 0.19
pyridoxal
0.01 - 0.03
pyridoxamine
0.025
pyridoxine
-
kinase 1 with MgATP2- as substrate, pH 7.3, 37°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2 - 2.3
pyridoxal
0.4 - 0.7
pyridoxamine
0.3
pyridoxine
-
kinase 1 with MgATP2- as substrate, pH 7.3, 37°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.052
-
purified kinase 2 enzyme, pH 6.1, 37°C
2.7
-
purified kinase 1 enzyme, pH 6.1, 37°C
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.14
-
kinase 1, calculated from the deduced amino acid sequence
6.05
-
kinase 2, calculated from the deduced amino acid sequence
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
biotransformation of pyridoxal to pyridoxal 5'-phosphate (PLP) by pyridoxal kinase (pdxY) supports cadaverine production in Escherichia coli. PLP is an essential cofactor of lysine decarboxylase and the major bottleneck in the cadaverine biosynthesis pathway
additional information
experimental resurrection of the last common ancestor of the hydroxymethyl pyrimidine kinase group based on comparison of hydroxymethyl pyrimidine and pyridoxal kinases. Probably the last common ancestor was not able to use pyridoxal under physiological conditions. The pyridoxal kinase activity present in the current bifunctional enzymes must have appeared in a convergent event independently of the pyridoxal kinase activity of pdxY and pdxK genes. Substrate pyridoxal is 8-times less preferred than the phosphorylation of hydroxymethyl pyrimidine by the last ancestor
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop vapour diffusion method using 20 mM potassium phosphate, pH 7.5, 5 mM beta-mercaptoethanol, 0.2 mM EDTA, and 21% PEG 4K, 100 mM Tris-HCl, pH 8.5, 200 mM Na acetate, 40 mM MgSO4, and 10% glycerol
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
K229Q
-
the mutant enzyme is not inhibited by pyridoxal
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-80°C, 20 mM phosphate buffer, pH 7.3, stable for at least some weeks
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Ni-NTA agarose column chromatography
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
gene pdxY, cloned into pET23a::pdxY (p23YH) or pET23a:: pdxK (p23KH) as a one-vector system in Escherichia coli strain DH5alpha and transformed into Escherichia coli strain BL21(DE3)
kinase 1 and 2 expressed in Escherichia coli HMS174(DE3), kinase 2 additionally expressed as His-tag fusion protein
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
synthesis
production of cadaverine (1,5-diaminopentane) can be done by fermentation or direct bioconversion and plays an important role as a building block of polyamides. Lysine decarboxylase (CadA) transforms L-lysine to cadaverine and pyridoxal 5'-phosphate (PLP) can increase the conversion rate and yield as a cofactor. Biotransformation of cadaverine using whole Escherichia coli cells that overexpress lysine decarboxylase has many merits, such as the rapid conversion of L-lysine to cadaverine, possible application of high concentration reactions up to the molar level, production of less byproduct, and potential reuse of the enzyme by immobilization. But the supply of PLP, an essential cofactor of lysine decarboxylase, is the major bottleneck in this system. Among various PLP systems examined, pyridoxal kinase (PdxY) shows the highest conversion of PL to PLP, resulting in more than 60 % conversion of L-lysine to cadaverine with lysine decarboxylase. Method evaluation and optimization. Interconversion of interconvertion of pyridoxal and pyridoxamine has to be controlled
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Yang, Y.; Tsui, H.C.; Man, T.K.; Winkler, M.E.
Identification and function of the pdxY gene, which encodes a novel pyridoxal kinase involved in the salvage pathway of pyridoxal 5'-phosphate biosynthesis in Escherichia coli K-12
J. Bacteriol.
180
1814-1821
1998
Escherichia coli
Manually annotated by BRENDA team
di Salvo, M.L.; Hunt, S.; Schirch, V.
Expression, purification, and kinetic constants for human and Escherichia coli pyridoxal kinases
Protein Expr. Purif.
36
300-306
2004
Escherichia coli, Homo sapiens (O00764), Homo sapiens
Manually annotated by BRENDA team
Safo, M.K.; Musayev, F.N.; di Salvo, M.L.; Hunt, S.; Claude, J.B.; Schirch, V.
Crystal structure of pyridoxal kinase from the Escherichia coli pdxK gene: implications for the classification of pyridoxal kinases
J. Bacteriol.
188
4542-4552
2006
Escherichia coli (P40191), Escherichia coli
Manually annotated by BRENDA team
di Salvo, M.L.; Nogues, I.; Parroni, A.; Tramonti, A.; Milano, T.; Pascarella, S.; Contestabile, R.
On the mechanism of Escherichia coli pyridoxal kinase inhibition by pyridoxal and pyridoxal 5-phosphate
Biochim. Biophys. Acta
1854
1160-1166
2015
Escherichia coli, Escherichia coli BW25113
Manually annotated by BRENDA team
Castro-Fernandez, V.; Bravo-Moraga, F.; Ramirez-Sarmiento, C.A.; Guixe, V.
Emergence of pyridoxal phosphorylation through a promiscuous ancestor during the evolution of hydroxymethyl pyrimidine kinases
FEBS Lett.
588
3068-3073
2014
Escherichia coli (P40191)
Manually annotated by BRENDA team
Kim, J.H.; Kim, J.; Kim, H.J.; Sathiyanarayanan, G.; Bhatia, S.K.; Song, H.S.; Choi, Y.K.; Kim, Y.G.; Park, K.; Yang, Y.H.
Biotransformation of pyridoxal 5-phosphate from pyridoxal by pyridoxal kinase (pdxY) to support cadaverine production in Escherichia coli
Enzyme Microb. Technol.
104
9-15
2017
Escherichia coli (P77150), Escherichia coli
Manually annotated by BRENDA team