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Information on EC 1.4.4.2 - glycine dehydrogenase (aminomethyl-transferring)
for references in articles please use BRENDA:EC1.4.4.2
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EC Tree 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)
IUBMB Comments
A pyridoxal-phosphate protein. A component of the glycine cleavage system, which is composed of four components that only loosely associate: the P protein (EC 1.4.4.2), the T protein (EC 2.1.2.10, aminomethyltransferase), the L protein (EC 1.8.1.4, dihydrolipoyl dehydrogenase) and the lipoyl-bearing H protein . Previously known as glycine synthase.
The enzyme appears in viruses and cellular organisms
- 1.4.4.2
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coil
- aneurysm
-
guglielmi
-
embolization
-
endovascular
- artery
- measles
-
occlusion
- cerebral
-
intracranial
- hemagglutinin
-
rupture
- neck
-
dental
-
subarachnoid
- hemorrhage
-
photorespiratory
-
angiographic
-
photorespiration
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council
- distemper
- hyperglycinemia
-
dentist
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lipoylation
- hydroxymethyltransferase
- polyomavirus
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angiogram
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t-proteins
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slam
-
lipoic
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nonketotic
-
rebleeding
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microcatheter
- morbillivirus
- vasospasm
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unruptured
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recanalization
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basilar
-
polyoma
-
ceria
- glycodeoxycholate
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practise
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procedure-related
- lipoamide
-
profession
- flaveria
- lipoate
- panencephalitis
- medicine
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postal
-
curriculum
Reaction Schemes
showSynonyms
gdc, h protein, h-protein, glycine decarboxylase, t protein, protein p1, h1 protein, glycine decarboxylase complex, glycine cleavage enzyme complex, h2 protein, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
decarboxylase, glycine
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GDC
GLDC
Glycine cleavage system P-protein
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glycine decarboxylase
glycine decarboxylase (P-protein)
glycine decarboxylase complex
glycine decarboxylase P-protein
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glycine dehydrogenase
glycine dehydrogenase (decarboxylating)
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glycine-cleavage complex
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P protein
P-protein
Protein P1
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-
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additional information
glycine decarboxylase, or P-protein, is part of the glycine cleavage system, GCS
GDC
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a four-protein system comprising three enzymes (P-protein, T-protein, and L-protein) plus H-protein
GDC
GDC is composed of four subunits, designated P-, H-, T-, and L-proteins, encoded by nuclear genes with N-terminal mitochondrial targeting pre-sequences, the Populus genome contains eight transcriptionally active GDC genes, encoding four H-proteins, two T-proteins, and single P- and L-proteins
glycine decarboxylase
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-
-
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glycine decarboxylase complex
the glycine decarboxylase complex cooperates with serine hydroxymethyltransferase to mediate photorespiratory glycine-serine interconversion
P-protein
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
glycine + [glycine-cleavage complex H protein]-N6-lipoyl-L-lysine = [glycine-cleavage complex H protein]-S-aminomethyl-N6-dihydrolipoyl-L-lysine + CO2
glycine + [glycine-cleavage complex H protein]-N6-lipoyl-L-lysine = [glycine-cleavage complex H protein]-S-aminomethyl-N6-dihydrolipoyl-L-lysine + CO2
mechanism
-
glycine + [glycine-cleavage complex H protein]-N6-lipoyl-L-lysine = [glycine-cleavage complex H protein]-S-aminomethyl-N6-dihydrolipoyl-L-lysine + CO2
mechanism
-
glycine + [glycine-cleavage complex H protein]-N6-lipoyl-L-lysine = [glycine-cleavage complex H protein]-S-aminomethyl-N6-dihydrolipoyl-L-lysine + CO2
H-protein ping-pong mechanism
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glycine + [glycine-cleavage complex H protein]-N6-lipoyl-L-lysine = [glycine-cleavage complex H protein]-S-aminomethyl-N6-dihydrolipoyl-L-lysine + CO2
sequential random bi bi mechanism in which no abortive dead end complex is formed
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glycine + [glycine-cleavage complex H protein]-N6-lipoyl-L-lysine = [glycine-cleavage complex H protein]-S-aminomethyl-N6-dihydrolipoyl-L-lysine + CO2
mechanism of the GLDC-catalyzed reaction, detailed overview. GLDC is an unusual PLP-containing alpha-amino acid decarboxylase that removes carbon dioxide from the glycine substrate without releasing the expected amine (methylamine, a metabolic precursor of toxic formaldehyde) as a product. In an unusual decarboxylation mechanism, the resulting aminomethyl moiety is instead transferred to an accessory H-protein. (1) H-Protein is not required for glycine decarboxylation but, instead, is required for the release of the aminomethyl moiety from the quinonoid adduct. (2) Glycine decarboxylation is reversible and presumably proceeds through a stable quinonoid intermediate. (3) The physiological product of glycine decarboxylation is H-protein-S-aminomethyl dihydrolipoyllysine and not methylamine (in the absence of H-protein, the aminomethyl moiety remains as a quinonoid adduct)
glycine + [glycine-cleavage complex H protein]-N6-lipoyl-L-lysine = [glycine-cleavage complex H protein]-S-aminomethyl-N6-dihydrolipoyl-L-lysine + CO2
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
decarboxylation
oxidation
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redox reaction
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reduction
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decarboxylation
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decarboxylation
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co-substrate is H-protein, a lipoid acid-containing protein
decarboxylation
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co-substrate is H-protein, a lipoid acid-containing protein
decarboxylation
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co-substrate is H-protein, a lipoid acid-containing protein
decarboxylation
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co-substrate is H-protein, a lipoid acid-containing protein
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PATHWAY SOURCE
PATHWAYS
MetaCyc
glycine biosynthesis II, glycine cleavage
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SYSTEMATIC NAME
IUBMB Comments
glycine:H-protein-lipoyllysine oxidoreductase (decarboxylating, acceptor-amino-methylating)
A pyridoxal-phosphate protein. A component of the glycine cleavage system, which is composed of four components that only loosely associate: the P protein (EC 1.4.4.2), the T protein (EC 2.1.2.10, aminomethyltransferase), the L protein (EC 1.8.1.4, dihydrolipoyl dehydrogenase) and the lipoyl-bearing H protein [3]. Previously known as glycine synthase.
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CAS REGISTRY NUMBER
COMMENTARY
37259-67-9
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
glycine + His-tagged H-apoprotein
?
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Substrates: very low activity
Products: -
Products: -
?
glycine + lipoylated H-apoprotein
?
-
Substrates: very low activity
Products: -
Products: -
?
glycine + lipoylated His-tagged H-apoprotein
?
-
Substrates: very low activity
Products: -
Products: -
?
glycine + [glycine-cleavage complex H protein]-N6-lipoyl-L-lysine
[glycine-cleavage complex H protein]-S-aminomethyl-N6-dihydrolipoyl-L-lysine + CO2
P2 protein-S-aminomethyldihydrolipoyl-L-lysine + bicarbonate
?
-
Substrates: -
Products: -
Products: -
r
glycine + H-protein-lipoyllysine
H-protein-S-aminomethyldihydrolipoyllysine + CO2
-
Substrates: -
Products: -
Products: -
?
glycine + H-protein-lipoyllysine
H-protein-S-aminomethyldihydrolipoyllysine + CO2
-
Substrates: -
Products: -
Products: -
?
glycine + H-protein-lipoyllysine
H-protein-S-aminomethyldihydrolipoyllysine + CO2
-
Substrates: -
Products: -
Products: -
?
glycine + H-protein-lipoyllysine
H-protein-S-aminomethyldihydrolipoyllysine + CO2
Substrates: -
Products: -
Products: -
?
glycine + H-protein-lipoyllysine
H-protein-S-aminomethyldihydrolipoyllysine + CO2
-
Substrates: -
Products: -
Products: -
?
glycine + H-protein-lipoyllysine
H-protein-S-aminomethyldihydrolipoyllysine + CO2
Substrates: -
Products: -
Products: -
?
glycine + H-protein-lipoyllysine
H-protein-S-aminomethyldihydrolipoyllysine + CO2
Substrates: P-protein is the actual glycine-decarboxylating enzyme and uses pyridoxal 5'-phosphate as a cofactor. CO2 is released in the reaction and the residual aminomethyl group is bound to the oxidized lipoamide arm of H-protein
Products: the methylene group is accepted by tetrahydrofolate to yield methylene tetrahydrofolate, a major cofactor in one-carbon metabolism
Products: the methylene group is accepted by tetrahydrofolate to yield methylene tetrahydrofolate, a major cofactor in one-carbon metabolism
?
glycine + H-protein-lipoyllysine
H-protein-S-aminomethyldihydrolipoyllysine + CO2
-
Substrates: -
Products: -
Products: -
?
glycine + H-protein-lipoyllysine
H-protein-S-aminomethyldihydrolipoyllysine + CO2
-
Substrates: -
Products: -
Products: -
?
glycine + lipoylprotein
S-aminomethyldihydrolipoylprotein + CO2
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Substrates: lipoyl protein: H-protein, lipoamide can also act as acceptor
Products: -
Products: -
?
glycine + lipoylprotein
S-aminomethyldihydrolipoylprotein + CO2
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Substrates: lipoyl protein: H-protein, lipoamide can also act as acceptor
Products: -
Products: -
?
glycine + lipoylprotein
S-aminomethyldihydrolipoylprotein + CO2
C3-plants
-
Substrates: -
Products: -
Products: -
?
glycine + lipoylprotein
S-aminomethyldihydrolipoylprotein + CO2
-
Substrates: -
Products: -
Products: -
?
glycine + lipoylprotein
S-aminomethyldihydrolipoylprotein + CO2
Substrates: -
Products: -
Products: -
?
glycine + lipoylprotein
S-aminomethyldihydrolipoylprotein + CO2
-
Substrates: reaction is stimulated by lipoic acid which is a functional group of the H-protein
Products: -
Products: -
?
glycine + lipoylprotein
S-aminomethyldihydrolipoylprotein + CO2
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Substrates: glycine decarboxylation catalyzed by P-protein alone is extremely low
Products: -
Products: -
?
glycine + lipoylprotein
S-aminomethyldihydrolipoylprotein + CO2
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Substrates: lipoyl protein: H-protein, lipoamide can also act as acceptor
Products: -
Products: -
?
glycine + lipoylprotein
S-aminomethyldihydrolipoylprotein + CO2
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Substrates: lipoyl protein: H-protein, lipoamide can also act as acceptor
Products: -
Products: -
?
glycine + lipoylprotein
S-aminomethyldihydrolipoylprotein + CO2
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Substrates: lipoyl protein: H-protein, lipoamide can also act as acceptor
Products: -
Products: -
?
glycine + lipoylprotein
S-aminomethyldihydrolipoylprotein + CO2
-
Substrates: -
Products: -
Products: -
?
glycine + lipoylprotein
S-aminomethyldihydrolipoylprotein + CO2
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Substrates: lipoyl protein: H-protein, lipoamide can also act as acceptor
Products: -
Products: -
?
glycine + lipoylprotein
S-aminomethyldihydrolipoylprotein + CO2
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Substrates: lipoyl protein: H-protein, lipoamide can also act as acceptor
Products: -
Products: -
?
glycine + lipoylprotein
S-aminomethyldihydrolipoylprotein + CO2
-
Substrates: -
Products: -
Products: -
?
glycine + lipoylprotein
S-aminomethyldihydrolipoylprotein + CO2
-
Substrates: lipoyl protein: H-protein, lipoamide can also act as acceptor
Products: -
Products: -
?
glycine + lipoylprotein
S-aminomethyldihydrolipoylprotein + CO2
-
Substrates: -
Products: -
Products: -
?
glycine + [glycine-cleavage complex H protein]-N6-lipoyl-L-lysine
[glycine-cleavage complex H protein]-S-aminomethyl-N6-dihydrolipoyl-L-lysine + CO2
Substrates: -
Products: -
Products: -
r
glycine + [glycine-cleavage complex H protein]-N6-lipoyl-L-lysine
[glycine-cleavage complex H protein]-S-aminomethyl-N6-dihydrolipoyl-L-lysine + CO2
Substrates: reversible reaction
Products: -
Products: -
r
additional information
?
-
-
Substrates: the GDC H-protein (GLDH) has no catalytic activity itself but interacts via its lipoyl arm one after the other with the three other GDC subunits, P-protein (EC 1.4.4.2), T-protein (EC 2.1.2.10), and L-protein (EC 1.8.1.4)
Products: -
Products: -
?
additional information
?
-
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Substrates: the GDC H-protein is a substrate for P-protein of glycine decarboxylase
Products: -
Products: -
?
additional information
?
-
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Substrates: P-protein also catalyzes exchange of carbonyl carbon of glycine with CO2, reaction greatly stimulated by addition of H protein
Products: -
Products: -
?
additional information
?
-
-
Substrates: P-protein also catalyzes exchange of carbonyl carbon of glycine with CO2, reaction greatly stimulated by addition of H protein
Products: -
Products: -
?
additional information
?
-
-
Substrates: the glycine cleavage system consists of 4 protein components: 1. P-protein is a pyridoxal containing protein: a Schiff base is formed between the hydroxyl group of the pyridoxal phosphate and the alpha-NH2 of glycine, the amino group and the alpha-carbon of the glycine are transferred to the lipoamide cofactor of the second enzyme of the complex the H-protein, the alpha-carbonyl group of glycine is lost as CO2, 2. H-protein, 3. T-protein: catalyzes the passage of alpha-carbon from lipoamide of H protein to tetrahydrofolate, alpha-NH2 from glycine is lost as NH4+, 4. L-protein: catalyzes oxidation of reduced lipoamide back to its original form with concomitant reduction of NAD+ to NADH
Products: -
Products: -
?
additional information
?
-
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Substrates: nonketotic hyperglycinaemia is an autosomal recessive disorder of glycine metabolism caused by a deficiency in the mitochondrial glycine cleavage enzyme. The majority of cases are caused by mutations in the P-protein
Products: -
Products: -
?
additional information
?
-
Substrates: presence of excess pyridoxal 5'-phosphate is used in the assay mixture to facilitate the displacement of the quinonoid intermediate in the absence of an acceptor for the methylamine moiety (of decarboxylated glycine) to allow multiple enzyme turnovers. Mass spectrometry and 13C NMR spectroscopy are used to determine the products of glycine decarboxylation. The assay reaction mixtures are incubated for 1 week at pH 7.0, 25°C
Products: -
Products: -
?
additional information
?
-
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Substrates: presence of excess pyridoxal 5'-phosphate is used in the assay mixture to facilitate the displacement of the quinonoid intermediate in the absence of an acceptor for the methylamine moiety (of decarboxylated glycine) to allow multiple enzyme turnovers. Mass spectrometry and 13C NMR spectroscopy are used to determine the products of glycine decarboxylation. The assay reaction mixtures are incubated for 1 week at pH 7.0, 25°C
Products: -
Products: -
?
additional information
?
-
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Substrates: glycine decarboxylase does not occur as a complex of all four proteins, but L-protein takes part in both glycine decarboxylase as well as in glycine reductase reaction
Products: -
Products: -
?
additional information
?
-
-
Substrates: P-protein also catalyzes exchange of carbonyl carbon of glycine with CO2, reaction greatly stimulated by addition of H protein
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is a component of the reversible glycine cleavage system, previously known as glycine synthase
Products: -
Products: -
?
additional information
?
-
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Substrates: in transgenic potato plants with an antisense reduction in P-protein of GDC, the decrease in photorespiratory decarboxylation is compensated for by an increase in respiratory decarboxylation in the light
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
glycine + [glycine-cleavage complex H protein]-N6-lipoyl-L-lysine
[glycine-cleavage complex H protein]-S-aminomethyl-N6-dihydrolipoyl-L-lysine + CO2
Substrates: -
Products: -
Products: -
r
glycine + H-protein-lipoyllysine
H-protein-S-aminomethyldihydrolipoyllysine + CO2
-
Substrates: -
Products: -
Products: -
?
glycine + H-protein-lipoyllysine
H-protein-S-aminomethyldihydrolipoyllysine + CO2
-
Substrates: -
Products: -
Products: -
?
glycine + H-protein-lipoyllysine
H-protein-S-aminomethyldihydrolipoyllysine + CO2
-
Substrates: -
Products: -
Products: -
?
glycine + H-protein-lipoyllysine
H-protein-S-aminomethyldihydrolipoyllysine + CO2
Substrates: -
Products: -
Products: -
?
glycine + H-protein-lipoyllysine
H-protein-S-aminomethyldihydrolipoyllysine + CO2
-
Substrates: -
Products: -
Products: -
?
glycine + H-protein-lipoyllysine
H-protein-S-aminomethyldihydrolipoyllysine + CO2
Substrates: P-protein is the actual glycine-decarboxylating enzyme and uses pyridoxal 5'-phosphate as a cofactor. CO2 is released in the reaction and the residual aminomethyl group is bound to the oxidized lipoamide arm of H-protein
Products: the methylene group is accepted by tetrahydrofolate to yield methylene tetrahydrofolate, a major cofactor in one-carbon metabolism
Products: the methylene group is accepted by tetrahydrofolate to yield methylene tetrahydrofolate, a major cofactor in one-carbon metabolism
?
glycine + H-protein-lipoyllysine
H-protein-S-aminomethyldihydrolipoyllysine + CO2
-
Substrates: -
Products: -
Products: -
?
glycine + H-protein-lipoyllysine
H-protein-S-aminomethyldihydrolipoyllysine + CO2
-
Substrates: -
Products: -
Products: -
?
glycine + lipoylprotein
S-aminomethyldihydrolipoylprotein + CO2
-
Substrates: lipoyl protein: H-protein, lipoamide can also act as acceptor
Products: -
Products: -
?
glycine + lipoylprotein
S-aminomethyldihydrolipoylprotein + CO2
-
Substrates: lipoyl protein: H-protein, lipoamide can also act as acceptor
Products: -
Products: -
?
glycine + lipoylprotein
S-aminomethyldihydrolipoylprotein + CO2
C3-plants
-
Substrates: -
Products: -
Products: -
?
glycine + lipoylprotein
S-aminomethyldihydrolipoylprotein + CO2
Substrates: -
Products: -
Products: -
?
glycine + lipoylprotein
S-aminomethyldihydrolipoylprotein + CO2
-
Substrates: reaction is stimulated by lipoic acid which is a functional group of the H-protein
Products: -
Products: -
?
glycine + lipoylprotein
S-aminomethyldihydrolipoylprotein + CO2
-
Substrates: glycine decarboxylation catalyzed by P-protein alone is extremely low
Products: -
Products: -
?
glycine + lipoylprotein
S-aminomethyldihydrolipoylprotein + CO2
-
Substrates: lipoyl protein: H-protein, lipoamide can also act as acceptor
Products: -
Products: -
?
glycine + lipoylprotein
S-aminomethyldihydrolipoylprotein + CO2
-
Substrates: lipoyl protein: H-protein, lipoamide can also act as acceptor
Products: -
Products: -
?
glycine + lipoylprotein
S-aminomethyldihydrolipoylprotein + CO2
-
Substrates: lipoyl protein: H-protein, lipoamide can also act as acceptor
Products: -
Products: -
?
glycine + lipoylprotein
S-aminomethyldihydrolipoylprotein + CO2
-
Substrates: -
Products: -
Products: -
?
glycine + lipoylprotein
S-aminomethyldihydrolipoylprotein + CO2
-
Substrates: lipoyl protein: H-protein, lipoamide can also act as acceptor
Products: -
Products: -
?
glycine + lipoylprotein
S-aminomethyldihydrolipoylprotein + CO2
-
Substrates: lipoyl protein: H-protein, lipoamide can also act as acceptor
Products: -
Products: -
?
glycine + lipoylprotein
S-aminomethyldihydrolipoylprotein + CO2
-
Substrates: -
Products: -
Products: -
?
glycine + lipoylprotein
S-aminomethyldihydrolipoylprotein + CO2
-
Substrates: lipoyl protein: H-protein, lipoamide can also act as acceptor
Products: -
Products: -
?
additional information
?
-
-
Substrates: nonketotic hyperglycinaemia is an autosomal recessive disorder of glycine metabolism caused by a deficiency in the mitochondrial glycine cleavage enzyme. The majority of cases are caused by mutations in the P-protein
Products: -
Products: -
?
additional information
?
-
-
Substrates: in transgenic potato plants with an antisense reduction in P-protein of GDC, the decrease in photorespiratory decarboxylation is compensated for by an increase in respiratory decarboxylation in the light
Products: -
Products: -
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pyridoxal 5'-phosphate
-
2 mol of pyridoxal phosphate bound per mol of enzyme
pyridoxal 5'-phosphate
-
binding to the apoenzyme induces large open-closed conformational changes, with residues moving up to 13.5 A
pyridoxal 5'-phosphate
P-protein is the actual glycine-decarboxylating enzyme and uses pyridoxal 5'-phosphate as a cofactor
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
aminoacetonitrile
the inhibitor of GDC is able to mimic mitochondrial depolarization, hydrogen peroxide production, and cell death in response to stress or harpin treatment of cultured Arabidopsis cells
Co2+
-
inhibition of glycine-CO2 exchange by binding of metal with H-protein-bound intermediate of glycine decarboxylation
Cu2+
-
inhibition of glycine-CO2 exchange by binding of metal with H-protein-bound intermediate of glycine decarboxylation
Fe2+
-
slight inhibition of glycine-CO2 exchange by binding of metal with H-protein-bound intermediate of glycine decarboxylation
harpin
the bacterial elicitor, a strong inducer of reactive oxygen species and NO, inhibits GDC activity
-
Modified H-protein
-
lipoic acid prosthetic group and cysteinyl residues modified with N-ethylmaleimide
-
Ni2+
-
inhibition of glycine-CO2 exchange by binding of metal with H-protein-bound intermediate of glycine decarboxylation
S-nitrosoglutathione
i.e. GSNO, the glycine decarboxylase complex, GDC activity is inhibited by S-nitrosoglutathione due to S-nitrosylation/S-glutathionylation of several cysteine residues, overview. The inhibition of GDC activity after GSNO treatment can be an indirect effect of ROS induced by inhibition of complex I
Zn2+
-
inhibition of glycine-CO2 exchange by binding of metal with H-protein-bound intermediate of glycine decarboxylation
additional information
-
inactivation after incubation with glycine in presence of aminomethyl carrier protein (H-protein), it is a suicide reaction of the P-protein as a side reaction of the glycine decarboxylation
-
additional information
-
inhibitors of the multienzyme complex
-
additional information
-
low CO2 concentrations decrease expression of GDC
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2-mercaptoethanol
-
thiol compound required for maximal activity on glycine-CO2 exchange reaction
GSH
-
thiol compound required for maximal activity on glycine-CO2 exchange reaction
H-protein
upon addition of exogenous unlipoylated H-protein, kcat increases 190fold, in the absence of the lipoic acid moiety on H-protein, the methylamine adduct with pyridoxal 5'-phosphate (aminomethyl-quinonoid intermediate) is released as the product of the GLDC-catalyzed decarboxylation of glycine
-
lipoylated H-protein
the presence of the lipoyl moiety on H-protein does not affect the rates of GLDC (or GLDCcoexp)-catalyzed glycine decarboxylation
-
dithiothreitol
-
thiol compound required for maximal activity on glycine-CO2 exchange reaction
dithiothreitol
-
P and H protein alone jointly catalyze the glycine-CO2 exchange reaction in presence of pyridoxal phosphate and dithiothreitol
additional information
the presence of the lipoyl moiety on H-protein does not affect the rates of GLDC (or GLDCcoexp)-catalyzed glycine decarboxylation further corroborates the suggestion that H-protein (or lipoylated H-protein) does not directly participate in and is not required for release of CO2 from glycine in the formation of the pyridoxal 5'-phosphate-quinonoid intermediate, an important distinction that is contrary to earlier findings
-
additional information
-
the presence of the lipoyl moiety on H-protein does not affect the rates of GLDC (or GLDCcoexp)-catalyzed glycine decarboxylation further corroborates the suggestion that H-protein (or lipoylated H-protein) does not directly participate in and is not required for release of CO2 from glycine in the formation of the pyridoxal 5'-phosphate-quinonoid intermediate, an important distinction that is contrary to earlier findings
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.043
Lipoamide
-
the apparent Km-value of rTvL for binding the free lipoamide
0.0026
rTvH1 protein
-
the apparent Km-value of rTvL for binding rTvH1
-
0.0037
rTvH2 protein
-
the apparent Km-value of rTvL for binding rTvH2
-
0.00031
glycine
pH 7.0, 25°C, recombinant coexpressed wild-type enzyme in presence of lipoylated H-protein
0.00037
glycine
pH 7.0, 25°C, recombinant coexpressed wild-type enzyme in presence of H-protein
1.3
glycine
pH 7.0, 25°C, recombinant individually expressed wild-type enzyme in presence of lipoylated H-protein
2.1
glycine
pH 7.0, 25°C, recombinant individually expressed wild-type enzyme in presence of H-protein
2.92
glycine
-
P-subunit in the presence of non-tagged lipoylated H-apoprotein, at pH 8
2.93
glycine
-
P-subunit in the presence of His-tagged non-lipoylated H-apoprotein, at pH 6
3.05
glycine
-
P-subunit in the presence of His-tagged lipoylated H-apoprotein, at pH 6
3.14
glycine
-
P-subunit in the presence of His-tagged lipoylated H-apoprotein, at pH 8
3.21
glycine
-
P-subunit in the presence of non-tagged lipoylated H-apoprotein, at pH 6