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Literature summary for 2.7.3.3 extracted from

  • Kang, L.; Shi, H.; Liu, X.; Zhang, C.; Yao, Q.; Wang, Y.; Chang, C.; Shi, J.; Cao, J.; Kong, J.; Chen, K.
    Arginine kinase is highly expressed in a resistant strain of silkworm (Bombyx mori, Lepidoptera): Implication of its role in resistance to Bombyx mori nucleopolyhedrovirus (2011), Comp. Biochem. Physiol. B, 158, 230-234.
    View publication on PubMed

Localization

Localization Comment Organism GeneOntology No. Textmining
cytoplasm main localization Bombyx mori 5737
-

Organism

Organism UniProt Comment Textmining
Bombyx mori Q2F5T5 lines NB, 306 and BC8
-

Purification (Commentary)

Purification (Comment) Organism
Ni2+-NTA column chromatography Bombyx mori

Source Tissue

Source Tissue Comment Organism Textmining
fat body
-
Bombyx mori
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larva
-
Bombyx mori
-
malpighian tubule
-
Bombyx mori
-
midgut
-
Bombyx mori
-
additional information not detected in hemocytes Bombyx mori
-
ovary
-
Bombyx mori
-
silk gland
-
Bombyx mori
-
testis
-
Bombyx mori
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + L-Arg
-
Bombyx mori ADP + Nomega-phospho-L-Arg
-
?

Synonyms

Synonyms Comment Organism
ATP: L-arginine phosphotransferase
-
Bombyx mori

Expression

Organism Comment Expression
Bombyx mori the expression level of the enzyme increases more than 10fold 24 h post inoculation of nucleopolyhedrovirus in Bombyx mori strains NB and BC8 up

General Information

General Information Comment Organism
physiological function arginine kinase is involved in the antiviral process of Bombyx mori larvae against nucleopolyhedrovirus infection Bombyx mori