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1.4.4.2: glycine dehydrogenase (aminomethyl-transferring)

This is an abbreviated version!
For detailed information about glycine dehydrogenase (aminomethyl-transferring), go to the full flat file.

Word Map on EC 1.4.4.2

Reaction

glycine
+
[glycine-cleavage complex H protein]-N6-lipoyl-L-lysine
=
[glycine-cleavage complex H protein]-S-aminomethyl-N6-dihydrolipoyl-L-lysine
+
CO2

Synonyms

decarboxylase, glycine, GDC, GDCP, GLDC, GLDH, GLDP, Gly decarboxylase complex, Gly decarboxylase H1, glycine cleavage enzyme complex, glycine cleavage H protein, glycine cleavage system H protein 1, Glycine cleavage system P-protein, glycine decarboxylase, glycine decarboxylase (P-protein), glycine decarboxylase complex, glycine decarboxylase complex H, glycine decarboxylase P-protein, glycine dehydrogenase, glycine dehydrogenase (decarboxylating), glycine-cleavage complex, H protein, H-protein, H1 protein, H2 protein, L protein, More, P protein, P-protein, P-protein (glycine decarboxylase), P-subunit, Protein P1, T protein

ECTree

     1 Oxidoreductases
         1.4 Acting on the CH-NH2 group of donors
             1.4.4 With a disulfide as acceptor
                1.4.4.2 glycine dehydrogenase (aminomethyl-transferring)

Posttranslational Modification

Posttranslational Modification on EC 1.4.4.2 - glycine dehydrogenase (aminomethyl-transferring)

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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
acetylation
the activity is regulated by sequential posttranslational modifications, including acetylation and polyubiquitination, and reveal critical regulatory mechanisms of glycine metabolism and tumorigenesis. Acetylation of K514 inhibits glycine catabolism and pyrimidine synthesis. In addition, this acetylation of glycine decarboxylase also primes for its K33-linked polyubiquitination and proteasomal degradation, leading to suppression of glycine metabolism and tumorigenesis
proteolytic modification
C3-plants
-
-
ubiquitination
the activity is regulated by sequential posttranslational modifications, including acetylation and polyubiquitination (K33-linked polyubiquitination), and reveal critical regulatory mechanisms of glycine metabolism and tumorigenesis