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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)

Engineering

Engineering on EC 1.4.4.2 - glycine dehydrogenase (aminomethyl-transferring)

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A389V
-
missense mutation, 6-8% of normal GLDC activity when expressed in COS7 cells
R739H
-
missense mutation, 6-8% of normal GLDC activity when expressed in COS7 cells
R998Q
homozygous mutation within the GLDC gene is detected in a neonate with the neonatal type of nonketotic hyperglycinemia
Mu0171
-
T protein mutant, from the gene sll0171, an internal 1 kb fragment is deleted and replaced by the aphll gene
Mu293
-
P protein mutant, from the gene slr0293, an internal 2.1 kb fragment is deleted and replaced by the aphll gene
Mu879
-
H protein mutant, from the gene slr0879, an internal 0.2 kb fragment is deleted and replaced by the aphll gene
additional information