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Information on EC 2.7.1.B20 - broad specificity nucleoside kinase and Organism(s) Methanocaldococcus jannaschii and UniProt Accession Q57849

for references in articles please use BRENDA:EC2.7.1.B20
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Methanocaldococcus jannaschii
UNIPROT: Q57849 not found.
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The taxonomic range for the selected organisms is: Methanocaldococcus jannaschii
The expected taxonomic range for this enzyme is: Bacteria, Archaea
Synonyms
nucleoside kinase, ta0880, mj0406, pfk-b sugar kinase, bth_i1158, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
NTP:nucleoside kinase
-
SYSTEMATIC NAME
IUBMB Comments
NTP:nucleoside 5'-phosphotransferase
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + cytidine
ADP + CMP
show the reaction diagram
at 70°C the Vmax/Km-value for cytidine is 93% of the Vmax/Km-value for inosine. At 50°C the Vmax/Km-value for cytidine is 59% of the Vmax/Km-value for inosine. Neither ADP, acetyl phosphate, nor diphosphate can replace ATP
-
-
?
ATP + guanosine
ADP + GMP
show the reaction diagram
at 70°C the Vmax/Km-value for guanosine is 52% of the Vmax/Km-value for inosine. At 50°C the Vmax/Km-value for guanosine is 52% of the Vmax/Km-value for inosine. Neither ADP, acetyl phosphate, nor diphosphate can replace ATP
-
-
?
ATP + inosine
ADP + IMP
show the reaction diagram
relative phosphoryl donor specificity: ATP (100%), ITP (41%), GTP (40%), UTP (8%), CTP (6%)
-
-
?
GTP + cytidine
GDP + CMP
show the reaction diagram
relative phosphoryl donor specificity: ATP (100%), ITP (41%), GTP (40%), UTP (8%), CTP (6%)
-
-
?
GTP + guanosine
GDP + GMP
show the reaction diagram
relative phosphoryl donor specificity: ATP (100%), ITP (41%), GTP (40%), UTP (8%), CTP (6%)
-
-
?
GTP + inosine
GDP + IMP
show the reaction diagram
relative phosphoryl donor specificity: ATP (100%), ITP (41%), GTP (40%), UTP (8%), CTP (6%)
-
-
?
ITP + cytidine
IDP + CMP
show the reaction diagram
relative phosphoryl donor specificity: ATP (100%), ITP (41%), GTP (40%), UTP (8%), CTP (6%)
-
-
?
ITP + guanosine
IDP + GMP
show the reaction diagram
relative phosphoryl donor specificity: ATP (100%), ITP (41%), GTP (40%), UTP (8%), CTP (6%)
-
-
?
ITP + inosine
IDP + IMP
show the reaction diagram
relative phosphoryl donor specificity: ATP (100%), ITP (41%), GTP (40%), UTP (8%), CTP (6%)
-
-
?
additional information
?
-
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
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Co2+
enzyme activity requires the presence of divalent cations. Mg2+ (100%) can be efficiently replaced by Mn2+ (97%) and partially by Ni2+ (31%) or Co2+ (6%)
Mn2+
enzyme activity requires the presence of divalent cations. Mg2+ (100%) can be efficiently replaced by Mn2+ (97%) and partially by Ni2+ (31%) or Co2+ (6%)
Ni2+
enzyme activity requires the presence of divalent cations. Mg2+ (100%) can be efficiently replaced by Mn2+ (97%) and partially by Ni2+ (31%) or Co2+ (6%)
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.017
cytidine
pH 7.0, 50°C, cosubstrate: ATP
0.062 - 0.078
guanosine
0.021
Inosine
pH 7.0, 50°C, cosubstrate: ATP
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.1 - 8.2
50% of maximal activity at pH 6.1 and at pH 8.2
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
the enzyme plays a role in nucleotide metabolism
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
34000
2 * 34000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
2 * 34000, SDS-PAGE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystallized as the apoenzyme as well as in complex with an ATP analogue and Mg2+. The latter crystal form is also soaked with D-fructose 6-phosphate. Synchrotron-radiation data are collected to 1.70 A for the apoenzyme crystals and 1.93 A for the complex crystals. All crystals exhibit orthorhombic symmetry. The apoenzyme crystals contain one monomer per asymmetric unit whereas the complex crystals contain a dimer
sitting- and hanging-drop vapour diffusion methods, three-dimensional structures of the unliganded enzyme and a complex of the enzyme, an ATP analogue and adenosine are determined to 1.7 and 1.9 A resolution, respectively. In the crystal structure of the MjNK complex, subunit A adopts a closed conformation and subunit B an open conformation. In subunit A all substrates and Mg2+ are observed, whereas in subunit B only the ATP analogue can be clearly identified in the electron density
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Arnfors, L.; Hansen, T.; Schnheit, P.; Ladenstein, R.; Meining, W.
Structure of Methanocaldococcus jannaschii nucleoside kinase: an archaeal member of the ribokinase family
Acta Crystallogr. Sect. D
62
1085-1097
2006
Methanocaldococcus jannaschii (Q57849), Methanocaldococcus jannaschii, Methanocaldococcus jannaschii DSM 2661 (Q57849)
Manually annotated by BRENDA team
Arnfors, L.; Hansen, T.; Meining, W.; Schnheit, P.; Ladenstein, R.
Expression, purification, crystallization and preliminary X-ray analysis of a nucleoside kinase from the hyperthermophile Methanocaldococcus jannaschii
Acta Crystallogr. Sect. F
61
591-594
2005
Methanocaldococcus jannaschii (Q57849), Methanocaldococcus jannaschii
Manually annotated by BRENDA team
Hansen, T.; Arnfors, L.; Ladenstein, R.; Schnheit, P.
The phosphofructokinase-B (MJ0406) from Methanocaldococcus jannaschii represents a nucleoside kinase with a broad substrate specificity
Extremophiles
11
105-114
2006
Methanocaldococcus jannaschii (Q57849), Methanocaldococcus jannaschii, Methanocaldococcus jannaschii DSM 2661 (Q57849)
Manually annotated by BRENDA team