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IUBMB Comments This is a heterogeneous group of serine/threonine protein kinases that do not have an activating compound and are either non-specific or their specificity has not been analysed to date.
The taxonomic range for the selected organisms is: Saccharolobus solfataricus The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
+
a [protein]-(L-serine/L-threonine)
=
+
a [protein]-(L-serine/L-threonine) phosphate
Synonyms
protein kinase a, 14-3-3, camkii, p-akt, lrrk2, c-jun n-terminal kinase, serine/threonine kinase, raf-1, protein kinase b, gsk-3,
more
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A-T, mutated homolog
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AMH type II receptor
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Anti-sigma B factor rsbT
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Ataxia telangiectasia mutated
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Ataxia telangiectasia mutated homolog
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ATP-protein transphosphorylase
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Breast-tumor-amplified kinase
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Calcium-dependent protein kinase C
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Calcium/phospholipid-dependent protein kinase
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cAMP-dependent protein kinase A
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CDC25 suppressing protein kinase
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Cell division cycle 2-like
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CLP-36 interacting kinase
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cyclic monophosphate-dependent protein kinase
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cyclic nucleotide-dependent protein kinase
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cyclin-dependent kinase
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cytidine 3',5'-cyclic monophosphate-responsive protein kinase
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hydroxyalkyl-protein kinase
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Kinase interacting with stathmin
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kinase, casein (phosphorylating)
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kinase, protamine (phosphorylating)
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kinase, protein (phosphorylating)
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kinase, protein, A (phosphorylating)
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kinase, protein, C (phosphorylating)
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Lymphocyte-oriented kinase
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M phase-specific cdc2 kinase
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membrane-associated protein-serine/threonine kinase
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mitogen-activated S6 kinase
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Myristoylated and palmitoylated serine-threonine kinase
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NY-REN-55 antigen
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phosphorylase b kinase kinase
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Pre-mRNA protein kinase
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protein glutamyl kinase
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protein kinase (phosphorylating)
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Protein kinase B kinase
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protein kinase CK2
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Protein kinase Krct
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Protein kinase MST
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protein kinase p58
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Protein kinase PKL12
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protein phosphokinase
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protein serine kinase
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protein serine-threonine kinase
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protein-aspartyl kinase
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protein-cysteine kinase
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protein-serine kinase
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protein-serine/threonine kinase
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proteinserine/threonine kinase
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PRP4 pre-mRNA processing factor 4 homolog
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ribosomal protein S6 kinase II
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ribosomal S6 protein kinase
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S-receptor kinase
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serine protein kinase
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serine(threonine) protein kinase
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serine-specific protein kinase
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serine/threonine kinase
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Serine/threonine kinase 15
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Serine/threonine kinase Ayk1
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serine/threonine protein kinase
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Serine/threonine-protein kinase NRK2
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Serine/threonine-protein kinase NYD-SPK
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Ste20-like kinase
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STE20-like kinase MST1
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STE20-like kinase MST2
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STE20-like kinase MST3
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Switch protein/serine kinase
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threonine-specific protein kinase
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type-2 casein kinase
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phospho group transfer
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ATP:protein phosphotransferase (non-specific)
This is a heterogeneous group of serine/threonine protein kinases that do not have an activating compound and are either non-specific or their specificity has not been analysed to date.
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191808-15-8
phosphoinositide dependent protein kinase 1
377752-08-4
ribosomal protein S6 kinase 2
389133-24-8
ribosomal S6 kinase 3
52660-18-1
casein kinase, protein kinase CK2
9026-43-1
this CAS Reg. No. encompasses a great variety of protein kinases including the serine/threonine specific kinases
90698-26-3
ribosomal protein S6 kinase 1
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ATP + a protein
ADP + a phosphoprotein
protein kinase activity, with a noticeable preference for phosphorylating proteins of acidic character. No activity with basic proteins such as histones or myelin basic protein. The protein kinase also can phosphorylate itself on serine and threonine residues. No autophosphorylation of the protein kinase can be detected prior to addition of exogenous substrate proteins. Thr-151 is a site of autophosphorylation, and that autophosphorylation of this residue enhances the catalytic efficiency of the enzyme
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-
?
ATP + casein
ADP + phopshorylated cysein
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-
?
ATP + reduced carboxymethylated lysozyme
ADP + phopshorylated reduced carboxymethylated lysozyme
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?
ADP + casein
AMP + phosphorylated casein
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phosphorylated on threonine residues
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-
?
ATP + a protein
ADP + a phosphoprotein
ATP + bovine serum albumin
ADP + phosphorylated bovine serum albumin
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?
ATP + casein
ADP + phosphocasein
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?
ATP + casein
ADP + phosphorylated casein
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phosphorylated on threonine residues
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?
ATP + histone
ADP + phosphorylated histone
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?
ATP + histone H4
ADP + phosphorylated histone H4
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phosphorylated on threonine and on serine residues
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?
ATP + KKRAARASSNVFA
ADP + ?
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phosphorylation of the peptide is undetectable at 25°C. Phosphorylation takes place at measurable rates if the assay temperature is raised to 65°C or if poly(Glu4:Tyr) is included in the assay mixture
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?
ATP + KKRAARATSNVFA
ADP + KKRAARApTSNVFA
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?
ATP + lysozyme
ADP + phopshorylated lysozyme
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reduced carboxyamidomethylated and maleylated lysozyme
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?
ATP + myelin basic protein
ADP + phosphorylated myelin basic protein
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?
ATP + partially dephosphorylated casein
ADP + ?
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?
ATP + reduced carboxyamidomethylated and maleylated lysozyme
ADP + phosphorylated reduced carboxyamidomethylated and maleylated lysozyme
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phosphorylated on threonine residues
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?
GDP + casein
GMP + phosphorylated casein
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phosphorylated on threonine residues
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?
GTP + casein
GDP + phosphorylated casein
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phosphorylated on threonine residues
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?
GTP + partially dephosphorylated casein
GDP + ?
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the enzyme catalyzes the transfer of phosphate from GTP at approximately two-thirds the rate observed with ATP
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?
additional information
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ATP + a protein
ADP + a phosphoprotein
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?
ATP + a protein
ADP + a phosphoprotein
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phosphorylation of exogenous substrates takes place on serine and, occasionally, threonine, but the enzyme displays a strong preference for threonine as the phospho-acceptor amino acid residue, overview, no activity with GTP except for the autophosphorylation reaction in vitro which functions with GTP and also GDP
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ATP + a protein
ADP + a phosphoprotein
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PK2 phosphorylate itself as well as several exogenous proteins, including mixed histones, casein, bovine serum albumin, and reduced carboxyamidomethylated and maleylated lysozyme, on serine residues, overview, autophosphorylation of rSsoPK2 can be uncoupled from the phosphorylation of exogenous proteins by manipulation of the temperature or mutagenic alteration of the enzyme, autophosphorylation is detected only at temperatures above 60°C, whereas phosphorylation of exogenous proteins is detectable at 37°C
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?
additional information
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the enzyme performs autophosphorylation in vitro
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?
additional information
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neither of the pyrimidine nucleotide triphosphates tested, CTP and UTP, serves as substrates and neither does AMP, GMP, or pyrophosphate
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?
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ATP + a protein
ADP + a phosphoprotein
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?
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additional information
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no activity with GTP
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Mg2+
activity requires the presence of a divalent metal ion cofactor. Mn2+ is most effective at supporting protein kinase activity. Mg2+ is moderately effective, while Ca2+, Ni2+, and Zn2+ are ineffective as cofactors
Mn2+
activity requires the presence of a divalent metal ion cofactor. Mn2+ is most effective at supporting protein kinase activity. Mg2+ is moderately effective, while Ca2+, Ni2+, and Zn2+ are ineffective as cofactors
Ca2+
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can only poorly substitute for Mn2+
Ni2+
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can only poorly substitute for Mn2+
Zn2+
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can only partially substitute for Mn2+
Mg2+
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less effective than Mn2+
Mg2+
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potential divalent metal ion cofactors Mn2+ and Mg2+
Mn2+
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preferred metal ion cofactor
Mn2+
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preferred metal ion cofactor, especially for the autophosphorylation reaction
Mn2+
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potential divalent metal ion cofactors Mn2+ and Mg2+
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1-(5-chloronaphthalene-1-sulfonyl)-1H-hexahydro-1,4-diazepine
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i.e. ML-9, 0.5-1.0 mM, 50% inhibition
1-(5-isoquinolinylsulfonyl)-2-methylpiperazine
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i.e. H-7
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5'-AMP
activity is increased several-fold upon preincubation with millimolar concentrations of 5'-AMP. Activation is enhanced by the presence of ATP
ADPribose
activity is increased several-fold upon preincubation with submicromolar concentrations of ADPribose. Activation is enhanced by the presence of ATP. ADP-ribose acts by evoking a conformational transition in the enzyme. Other mono- and di-nucleotides are ineffective
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0.02
KKRAARASSNVFA
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pH 6.5, 65°C
0.013 - 0.045
KKRAARATSNVFA
0.00074
ATP
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pH 6.5, 25°C
0.0157
ATP
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pH 6.5, 65°C
0.013
KKRAARATSNVFA
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pH 6.5, 25°C, presence of poly(Glu4:Tyr)
0.03
KKRAARATSNVFA
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pH 6.5, 25°C
0.045
KKRAARATSNVFA
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pH 6.5, 65°C
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0.5
tamoxifen
Saccharolobus solfataricus
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pH 6.5, 35°C, recombinant enzyme
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0.0024
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pH 6.5, 25°C, substrate: casein
additional information
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substrate specificity of the recombinant enzyme, overview
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37
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phosophorylation of exogenous proteins
60
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above, autophosphorylation activity
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5.7
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PK3, isoelectric focusing
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UniProt
brenda
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brenda
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membrane-associated
brenda
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associated
brenda
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62000
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x * 67000, glycosylated enzyme, SDS-PAGE, x * 62000, deglycosylated enzyme, SDS-PAGE
67000
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2 * 67000, SDS-PAGE
67000
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x * 67000, glycosylated and phosphorylated PK3, SDS-PAGE
67000
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x * 67000, glycosylated enzyme, SDS-PAGE, x * 62000, deglycosylated enzyme, SDS-PAGE
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dimer
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2 * 67000, SDS-PAGE
additional information
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enzyme domain structure analysis
?
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x * 67000, glycosylated and phosphorylated PK3, SDS-PAGE
?
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x * 67000, glycosylated enzyme, SDS-PAGE, x * 62000, deglycosylated enzyme, SDS-PAGE
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glycoprotein
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the glycosylated enzyme binds to Galanthus nivalis agglutinin
phosphoprotein
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the enzyme performs autophosphorylation at Ser548, determination of sites of autophosphorylation by mass spectrometry in two areas, one immediately N terminal to the region corresponding to subdomain I of eukaryotic protein kinases, and the second N terminal to the presumed activation loop located between subdomains VII and VIII, autophosphorylation of rSsoPK2 can be uncoupled from the phosphorylation of exogenous proteins by manipulation of the temperature or mutagenic alteration of the enzyme, autophosphorylation is detected only at temperatures above 60°C, whereas phosphorylation of exogenous proteins is detectable at 37°C
phosphoprotein
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the enzyme performs autophosphorylation in vitro
phosphoprotein
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the protein kinase undergoes autophosphorylation on threonine
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T151A
activity with reduced carboxymethylated lysozyme is much lower than wild-type activity. The stoichiometry of autophosphorylation is roughly half that of the unmodified protein
T151D
activity with reduced carboxymethylated lysozyme is much lower than wild-type activity. The stoichiometry of autophosphorylation is roughly half that of the unmodified protein
D349A
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site-directed mutagenesis, inactive mutant
D394A
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site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-tpe enzyme
K215A
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site-directed mutagenesis, inactive mutant
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native enzyme from membranes partially by detergent solubilization and anion exchange chromatography
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native enzyme partially by detergent solublization from membranes and anion exchange chromatography
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ORF sso0469, amino acid sequence determination and analysis, expression of wild-type and mutant enzymes in Escherichia coli
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orf sso2387, DNA and amino acid sequence determination and analysis, expression in Escherichia coli strain BL21(DE3) in inclusion bodies
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solubilization from inclusion bodies after recombinant expression in Escherichia coli by treatment with 5 M urea
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Lower, B.H.; Kennelly, P.J.
The membrane-associated protein-serine/threonine kinase from Sulfolobus solfataricus is a glycoprotein.
J. Bacteriol.
184
2614-2619
2002
Saccharolobus solfataricus
brenda
Lower, B.H.; Kennelly, P.J.
Open reading frame sso2387 from the archaeon Sulfolobus solfataricus encodes a polypeptide with protein-serine kinase activity
J. Bacteriol.
185
3436-3445
2003
Saccharolobus solfataricus
brenda
Lower, B.H.; Potters, M.B.; Kennelly, P.J.
A phosphoprotein from the archaeon Sulfolobus solfataricus with protein-serine/threonine kinase activity
J. Bacteriol.
186
463-472
2004
Saccharolobus solfataricus, Saccharolobus solfataricus P2
brenda
Lower, B.H.; Bischoff, K.M.; Kennelly, P.J.
The archaeon Sulfolobus solfataricus contains a membrane-associated protein kinase activity that preferentially phosphorylates threonine residues in vitro
J. Bacteriol.
182
3452-3459
2000
Saccharolobus solfataricus
brenda
Bischoff, K.M.; Kennelly, P.J.
In-gel assay for identifying alternative nucleotide substrates for protein kinases
Anal. Biochem.
271
199-202
1999
Saccharolobus solfataricus
brenda
Haile, J.D.; Kennelly, P.J.
The activity of an ancient atypical protein kinase is stimulated by ADP-ribose in vitro
Arch. Biochem. Biophys.
511
56-63
2011
Saccharolobus solfataricus (Q97ZY9), Saccharolobus solfataricus, Saccharolobus solfataricus P2 (Q97ZY9)
brenda
Transporter Classification Database (TCDB):
8.A.23.1.35 ,
9.B.321.1.1 ,
8.A.104.1.10 ,
1.A.87.2.4 ,
1.I.1.1.3 ,
1.A.87.2.9 ,
8.A.104.1.1 ,
1.A.87.2.6 ,
1.I.1.1.5 ,
9.A.15.1.1 ,
1.A.4.5.8 ,
1.A.4.5.1 ,
1.A.87.2.11 ,
8.A.104.1.9 ,
1.A.87.2.3 ,
8.A.104.1.5 ,
2.A.133.1.3