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Literature summary for 3.6.1.68 extracted from

  • Liu, J.; Guan, Z.; Liu, H.; Qi, L.; Zhang, D.; Zou, T.; Yin, P.
    Structural insights into the substrate recognition mechanism of Arabidopsis GPP-bound NUDX1 for noncanonical monoterpene biosynthesis (2018), Mol. Plant, 11, 218-221 .
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
hanging drop vapor diffusion method, using Arabidopsis thaliana

Protein Variants

Protein Variants Comment Organism
E56A inactive Arabidopsis thaliana
F127N the mutant shows reduced activity compared to the wild type enzyme Arabidopsis thaliana
F127N/P129N the mutant shows reduced activity compared to the wild type enzyme Arabidopsis thaliana
F134N the mutation decreases the enzyme activity by nearly half or more Arabidopsis thaliana
F134N the mutation leads to severely compromised hydrolase activity toward geranyl diphosphate Arabidopsis thaliana
F78N the mutant shows reduced activity compared to the wild type enzyme Arabidopsis thaliana
F85N the mutation decreases the enzyme activity by nearly half or more Arabidopsis thaliana
H42A the mutant shows strongly reduced activity compared to the wild type enzyme Arabidopsis thaliana
H49A the mutation exhibits little effect on the catalytic reaction Arabidopsis thaliana
L38N the mutant shows reduced activity compared to the wild type enzyme Arabidopsis thaliana
L45N the mutation leads to severely compromised hydrolase activity toward geranyl diphosphate Arabidopsis thaliana
P129N the mutant shows reduced activity compared to the wild type enzyme Arabidopsis thaliana
P136N the mutation exhibits little effect on the catalytic reaction Arabidopsis thaliana
P136N the mutation leads to severely compromised hydrolase activity toward geranyl diphosphate Arabidopsis thaliana
R27A the mutant shows strongly reduced activity compared to the wild type enzyme Arabidopsis thaliana
R34A the mutation leads to severely compromised hydrolase activity toward geranyl diphosphate Arabidopsis thaliana
V10K the mutation leads to the dissociation of the enzyme dimer Arabidopsis thaliana
V13N the mutant shows reduced activity compared to the wild type enzyme Arabidopsis thaliana
V20N the mutation decreases the enzyme activity by nearly half or more Arabidopsis thaliana
Y87A the mutant shows strongly reduced activity compared to the wild type enzyme Arabidopsis thaliana
Y94A the mutation leads to severely compromised hydrolase activity toward geranyl diphosphate Arabidopsis thaliana

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
geranyl diphosphate + H2O Arabidopsis thaliana
-
geranyl phosphate + phosphate
-
?

Organism

Organism UniProt Comment Textmining
Arabidopsis thaliana
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
geranyl diphosphate + H2O
-
Arabidopsis thaliana geranyl phosphate + phosphate
-
?

Subunits

Subunits Comment Organism
dimer
-
Arabidopsis thaliana

Synonyms

Synonyms Comment Organism
Nudix1
-
Arabidopsis thaliana
NUDX1
-
Arabidopsis thaliana