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Literature summary for 6.3.1.2 extracted from

  • Qiu, C.; Hong, Y.; Cao, Y.; Wang, F.; Fu, Z.; Shi, Y.; Wei, M.; Liu, S.; Lin, J.
    Molecular cloning and characterization of glutamine synthetase, a tegumental protein from Schistosoma japonicum (2012), Parasitol. Res., 111, 2367-2376.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
from 21-day schistosomes, DNA and amino acid sequence determination and analysis, sequence comparison, phylogenetic tree, quantitative real-time PCR expression analysis, expression of His-tagged enzyme in Escherichia coli strain BL21 (DE3) Schistosoma japonicum

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Schistosoma japonicum

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
40700
-
x * 45000, recombinant enzyme, SDS-PAGE, x * 40700, about, sequence calculation Schistosoma japonicum
45000
-
x * 45000, recombinant enzyme, SDS-PAGE, x * 40700, about, sequence calculation Schistosoma japonicum

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + L-glutamate + NH3 Schistosoma japonicum
-
ADP + phosphate + L-glutamine
-
?

Organism

Organism UniProt Comment Textmining
Schistosoma japonicum Q86EI1 Chinese mainland strain, Anhui isolate
-

Purification (Commentary)

Purification (Comment) Organism
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by affinity chromatography Schistosoma japonicum

Source Tissue

Source Tissue Comment Organism Textmining
integument in 28-day adult worms Schistosoma japonicum
-
additional information schistosomes are maintained in New Zealand rabbits. Quantitative real-time PCR expression analysis of enzyme in worms of different stages, overview Schistosoma japonicum
-
parenchyma in 28-day adult worms Schistosoma japonicum
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
3300
-
purified recombinant enzyme, pH 7.9, 37°C Schistosoma japonicum

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + L-glutamate + NH3
-
Schistosoma japonicum ADP + phosphate + L-glutamine
-
?

Subunits

Subunits Comment Organism
? x * 45000, recombinant enzyme, SDS-PAGE, x * 40700, about, sequence calculation Schistosoma japonicum

Synonyms

Synonyms Comment Organism
Glutamine synthetase
-
Schistosoma japonicum

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
assay at Schistosoma japonicum

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
25 40 purified recombinant enzyme, stable Schistosoma japonicum
50
-
purified recombinant enzyme, enzyme activity decreases rapidly at 50°C Schistosoma japonicum

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
-
Schistosoma japonicum

pH Stability

pH Stability pH Stability Maximum Comment Organism
6 9 purified recombinant enzyme, stable Schistosoma japonicum

Cofactor

Cofactor Comment Organism Structure
ATP
-
Schistosoma japonicum

Expression

Organism Comment Expression
Schistosoma japonicum transcription of SjGS is upregulated in praziquantel-treated worms at 2-, 4-, and 24-h posttreatment up

General Information

General Information Comment Organism
additional information the enzyme sequence contains a classic beta-grasp domain and a catalytic domain of glutamine synthetase Schistosoma japonicum
physiological function glutamine synthetase catalyzes the synthesis of glutamine, providing nitrogen for the production of purines, pyrimidines, amino acids, and other compounds required in many pivotal cellular events. The enzyme is important in the development of the schistosome Schistosoma japonicum