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Literature summary for 2.1.1.319 extracted from

  • Plett, K.; Raposo, A.; Bullivant, S.; Anderson, I.; Piller, S.; Plett, J.
    Root morphogenic pathways in Eucalyptus grandis are modified by the activity of protein arginine methyltransferases (2017), BMC Plant Biol., 17, 62 .
    View publication on PubMedView publication on EuropePMC
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Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2 S-adenosyl-L-methionine + [beta-tubulin]-L-arginine Eucalyptus grandis
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 2 S-adenosyl-L-homocysteine + [beta-tubulin]-Nomega,Nomega-dimethyl-L-arginine
-
 ?

Organism

Organism UniProt Comment Textmining
Eucalyptus grandis
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2 S-adenosyl-L-methionine + [beta-tubulin]-L-arginine
-
 Eucalyptus grandis 2 S-adenosyl-L-homocysteine + [beta-tubulin]-Nomega,Nomega-dimethyl-L-arginine
-
 ?

Synonyms

Synonyms Comment Organism
Eucgr.C03665.1
-
 Eucalyptus grandis
PRMT1
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 Eucalyptus grandis

General Information

General Information Comment Organism
physiological function the enzyme (PRMT1) methylate a number of key proteins and alters the transcription of a variety of genes involved in developmental processes. Appropriate levels of expression of type I PRMTs are necessary for the proper growth and development of Eucalyptus grandis roots. The enzyme (PRMT1) has a key role in root hair initiation and elongation and is involved in the methylation of beta-tubulin, a key protein in cytoskeleton formation Eucalyptus grandis