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Information on EC 2.7.1.40 - pyruvate kinase and Organism(s) Cryptosporidium parvum and UniProt Accession Q5CSM7

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EC Tree
IUBMB Comments
UTP, GTP, CTP, ITP and dATP can also act as donors. Also phosphorylates hydroxylamine and fluoride in the presence of CO2.
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Cryptosporidium parvum
UNIPROT: Q5CSM7
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Word Map
The taxonomic range for the selected organisms is: Cryptosporidium parvum
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
pyruvate kinase, m2-pk, pyruvate kinase m2, l-pk, pyk, tum2-pk, pyruvate kinase type m2, liver pyruvate kinase, pyruvate kinase m2 isoform, m2-pyruvate kinase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
CTHBP
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-
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cytosolic thyroid hormone binding protein
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-
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fluorokinase
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-
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kinase, fluoro- (phosphorylating)
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-
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kinase, pyruvate (phosphorylating)
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-
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L-PK
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-
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phosphoenol transphosphorylase
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phosphoenolpyruvate kinase
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pyruvate kinase muscle isozyme
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pyruvate phosphotransferase
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pyruvic kinase
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R-type/L-type pyruvate kinase
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red cell/liver pyruvate kinase
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THBP1
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-
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VEG17
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-
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vegetative protein 17
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-
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-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phospho group transfer
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-
-
-
SYSTEMATIC NAME
IUBMB Comments
ATP:pyruvate 2-O-phosphotransferase
UTP, GTP, CTP, ITP and dATP can also act as donors. Also phosphorylates hydroxylamine and fluoride in the presence of CO2.
CAS REGISTRY NUMBER
COMMENTARY hide
9001-59-6
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + pyruvate
ADP + phosphoenolpyruvate
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 + pyruvate
ADP + phosphoenolpyruvate
show the reaction diagram
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
sulfate
each monomer in the asymmetric unit of CpPyK binds two sulfate ions at equivalent positions, one in the C-domain and the other at the interface of the A and C domains, binding structure, overview. The sulfate ion in the C-domain occupies a position corresponding to the 6-phosphate of the effector molecule in different PyKs
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.5 - 7.5
activity range
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
pyruvate kinase of Cryptosporidium parvum is exceptional among known enzymes of protozoan origin in that it exhibits no allosteric property in the presence of commonly known effector molecules, mainly phosphosugars, due to blockage of the effector binding site by a sulfate ion, overview
additional information
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
tetramer
three-dimensional structure determination and analysis, structure comparisons, overview. Each CpPyK monomer consists of four domains: N (residues 23-32), A (residues 42-112 and 212-389), B (residues 113-211) and C (residues 390-526). The A-domain constitutes the central part of the molecule and forms a parallel (alphaa/beta)8 barrel. The B-domain contains nine beta strands that form an antiparallel beta-barrel. The active site is located at the interface of the A and B domains, and residues from both domains participate in substrate binding. The C-domain is composed of five beta strands surrounded by five alpha-helices. The allosteric site for binding the effector molecule is located in the C-domain. The A domains of the two monomers A and B form the major interface
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant untagged enzyme in apoform or complexed with the non-hydrolyzable ATP analogue adenyl-5'-yl imidodiphosphate, hanging drop vapor diffusion technique, 4°C, mixing of 7 mg/ml protein in 0.65 M ammonium sulfate and 0.1 M sodium acetate, pH 4.0, and with 3 mM adenyl-5'-yl imidodiphosphate, 5 mM magnesium chloride, and 5 mM pyruvic acid for the enzyme complex, X-ray diffraction structure determination and analysis at 2.5 A resolution, molecular replacement
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinnat enzyme from Eschericchia coli strain BL21(DE3) by ammonium sulfate fractionation, anion exchange chromatography, and gel filtration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli strain BL21(DE3)
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Cook, W.J.; Senkovich, O.; Aleem, K.; Chattopadhyay, D.
Crystal structure of Cryptosporidium parvum pyruvate kinase
PLoS ONE
7
e46875
2012
Cryptosporidium parvum (Q5CSM7), Cryptosporidium parvum
Manually annotated by BRENDA team