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Literature summary for 2.7.4.6 extracted from

  • Johansson, M.; Mackenzie-Hose, A.; Andersson, I.; Knorpp, C.
    Structure and mutational analysis of a plant mitochondrial nucleoside diphosphate kinase. Identification of residues involved in serine phosphorylation and oligomerization (2004), Plant Physiol., 136, 3034-3042.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
expressed as His-tag fusion protein in Escherichia coli DH5alpha Pisum sativum

Protein Variants

Protein Variants Comment Organism
H117A activity almost completely abolished Pisum sativum
H117D/S119A activity almost completely abolished Pisum sativum
S119A reduced serine phosphorylation, only modest decrease of activity Pisum sativum
S69A 6% and 14% of wild type activity using dCDP or dTDP as substrate respectively, changes in subunit composition with increasing number of tetramers and dimers Pisum sativum
S69A/S119A activity almost completely abolished Pisum sativum

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.07
-
dTDP S69A mutant enzyme, 22°C Pisum sativum
0.08
-
dTDP S119A mutant enzyme, 22°C Pisum sativum
0.09
-
dCDP S69A mutant enzyme, 22°C Pisum sativum
0.1
-
dTDP wild type enzyme, 22°C Pisum sativum
0.2
-
dCDP wild type enzyme, 22°C Pisum sativum
0.28
-
dCDP S119A mutant enzyme, 22°C Pisum sativum

Localization

Localization Comment Organism GeneOntology No. Textmining
mitochondrion
-
Pisum sativum 5739
-

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ divalent cation required for catalysis, Mg2+ preferred over other ions Pisum sativum

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + NDP Pisum sativum contributes to the maintenance of the cellular pools of all nucleosides triphosphates, broad substrate specificity, in plants involved in different signaling pathways ADP + NTP
-
?

Organism

Organism UniProt Comment Textmining
Pisum sativum Q9SP13 L. cv Oregon sugarpod
-

Purification (Commentary)

Purification (Comment) Organism
recombinant protein using His-tag Pisum sativum

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
50
-
H117A mutant enzyme with dCDP as substrate, 22°C Pisum sativum
60
-
S69A/S119A mutant enzyme with dCDP as substrate, 22°C Pisum sativum
70
-
H117D/S119A mutant enzyme with dCDP as substrate, 22°C Pisum sativum
160
-
S69A mutant enzyme with dCDP as substrate, 22°C Pisum sativum
700
-
S69A mutant enzyme with dTDP as substrate, 22°C Pisum sativum
2400
-
S119A mutant enzyme with dCDP as substrate, 22°C Pisum sativum
2700
-
wild type enzyme with dCDP as substrate, 22°C Pisum sativum
3900
-
S119A mutant enzyme with dTDP as substrate, 22°C Pisum sativum
5100
-
wild type enzyme with dTDP as substrate, 22°C Pisum sativum

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + dCDP
-
Pisum sativum ADP + dCTP
-
?
ATP + dTDP
-
Pisum sativum ADP + dTTP
-
?
ATP + NDP
-
Pisum sativum ADP + NTP
-
?
ATP + NDP contributes to the maintenance of the cellular pools of all nucleosides triphosphates, broad substrate specificity, in plants involved in different signaling pathways Pisum sativum ADP + NTP
-
?

Subunits

Subunits Comment Organism
hexamer monomers are arranged as trimers of dimers, crystal structure analysis Pisum sativum

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
9
-
dCDP S69A mutant enzyme, 22°C Pisum sativum
17
-
dTDP S69A mutant enzyme, 22°C Pisum sativum
105
-
dCDP S119A mutant enzyme, 22°C Pisum sativum
106
-
dCDP wild type enzyme, 22°C Pisum sativum
120
-
dTDP S119A mutant enzyme, 22°C Pisum sativum
147
-
dTDP wild type enzyme, 22°C Pisum sativum