Information on EC 2.1.2.10 - aminomethyltransferase

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea

EC NUMBER
COMMENTARY
2.1.2.10
-
RECOMMENDED NAME
GeneOntology No.
aminomethyltransferase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
[protein]-S8-aminomethyldihydrolipoyllysine + tetrahydrofolate = [protein]-dihydrolipoyllysine + 5,10-methylenetetrahydrofolate + NH3
show the reaction diagram
-
-
-
-
[protein]-S8-aminomethyldihydrolipoyllysine + tetrahydrofolate = [protein]-dihydrolipoyllysine + 5,10-methylenetetrahydrofolate + NH3
show the reaction diagram
formation of a folate-binding cavity via the interaction of enzyme with H-protein
-
[protein]-S8-aminomethyldihydrolipoyllysine + tetrahydrofolate = [protein]-dihydrolipoyllysine + 5,10-methylenetetrahydrofolate + NH3
show the reaction diagram
tetrahydrofolate is bound near the center of the tripartite enzyme, lipoic acid is bound adjacent to the tetrahydrofolate binding pocket
-
[protein]-S8-aminomethyldihydrolipoyllysine + tetrahydrofolate = [protein]-dihydrolipoyllysine + 5,10-methylenetetrahydrofolate + NH3
show the reaction diagram
5-methyltetrahydrofolate is bound in a kinked shape with the pteridine group deeply buried into the hydrophobic pocket ant the glutamyl group pointed to the C-terminal side surface. R292 interacts through water molecules with the folate polyglutamate tail
P48728
[protein]-S8-aminomethyldihydrolipoyllysine + tetrahydrofolate = [protein]-dihydrolipoyllysine + 5,10-methylenetetrahydrofolate + NH3
show the reaction diagram
T-protein recognition of lipoyl protein substrate and reaction mechanism, overview. The reversible transfer of the methylene group between the lipoate and tetrahydrofolate proceeds through the electron relay-assisted iminium intermediate formation
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
C-N bond cleavage
-
-
-
-
methyl group transfer
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
glycine cleavage
-
Glycine, serine and threonine metabolism
-
Metabolic pathways
-
One carbon pool by folate
-
SYSTEMATIC NAME
IUBMB Comments
[protein]-S8-aminomethyldihydrolipoyllysine:tetrahydrofolate aminomethyltransferase (ammonia-forming)
A component, with EC 1.4.4.2 glycine dehydrogenase (decarboxylating) and EC 1.8.1.4, dihydrolipoyl dehydrogenanse, of the glycine cleavage system, formerly known as glycine synthase. The glycine cleavage system 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), the L protein (EC 1.8.1.4) and the lipoyl-bearing H protein [3].
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
aminomethyltransferase
-
-
Amt
-
-
-
-
GCVT
-
two isogenes: GCVT-1 and GCVT-2
glycine synthase
-
-
-
-
synthase, glycine
-
-
-
-
T protein
-
-
-
-
T-protein
-
-
-
-
T-protein component of glycine cleavage complex
-
-
tetrahydrofolate aminomethyltransferase
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
37257-08-2
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
recombinant enzyme, expressed in Escherichia coli BL21 (DE3)pLysS
-
-
Manually annotated by BRENDA team
strain OT3
-
-
Manually annotated by BRENDA team
strain OT3, expression in Escherichia coli
-
-
Manually annotated by BRENDA team
Pyrococcus horikoshii OT-3
strain OT3
-
-
Manually annotated by BRENDA team
Pyrococcus horikoshii OT-3
strain OT3, expression in Escherichia coli
-
-
Manually annotated by BRENDA team
male Wistar rats
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
physiological function
-
part of glycine cleavage system, serine metabolism
physiological function
-
aminomethyltransferase reversibly catalyzes the degradation of the aminomethyl moiety of glycine attached to the lipoate cofactor of H-protein, resulting in the production of ammonia, 5,10-methylenetetrahydrofolate, and dihydrolipoate-bearing H-protein in the presence of tetrahydrofolate
metabolism
-
aminomethyltransferase is a component of the T-protein, which is part of a multienzyme system composed of four proteins termed P-, H-, T-, and L-protein. T-protein/aminomethyltransferase degrades the aminomethyl moiety to ammonia and 5,10-methylentetrahydrofolate in the presence of tetrahydrofolate, leaving dihydrolipoate-bearing H-protein
additional information
-
T-protein in complex with dihydrolipoate-bearing H-protein and 5-methyltetrahydrofolate, a complex mimicking the ternary complex in the reverse reaction, shows a highly interacting intermolecular interface limited to a small area and the protein-bound dihydrolipoyllysine arm inserted into the active site cavity of the T-protein. Arg292 of the T-protein is essential for complex assembly
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
reduced H-protein + 5,10-methylene-tetrahydrofolate + NH4Cl
?
show the reaction diagram
-
-
-
-
?
reduced H-protein + 5,10-methylenetetrahydropteroyltetraglutamate + NH4Cl
?
show the reaction diagram
-
-
-
-
?
S-aminomethyldihydrolipoylprotein + (6S)-tetrahydrofolate
dihydrolipoylprotein + (6R)-5,10-methylenetetrahydrofolate + NH3
show the reaction diagram
-
-
-
-
?
S-aminomethyldihydrolipoylprotein + (6S)-tetrahydrofolate
dihydrolipoylprotein + (6R)-5,10-methylenetetrahydrofolate + NH3
show the reaction diagram
-
aminomethyl intermediate bound to the lipoate cofactor of H-protein
-
r
S-aminomethyldihydrolipoylprotein + (6S)-tetrahydrofolate
dihydrolipoylprotein + (6R)-5,10-methylenetetrahydrofolate + NH3
show the reaction diagram
-
decarboxylated glycine moiety attached to H-protein + tetrahydrofolate as substrates
-
r
S-aminomethyldihydrolipoylprotein + (6S)-tetrahydrofolate
dihydrolipoylprotein + (6R)-5,10-methylenetetrahydrofolate + NH3
show the reaction diagram
-
decarboxylated glycine moiety attached to H-protein + tetrahydrofolate as substrates
-
r
S-aminomethyldihydrolipoylprotein + (6S)-tetrahydrofolate
dihydrolipoylprotein + (6R)-5,10-methylenetetrahydrofolate + NH3
show the reaction diagram
-
T-protein catalyzes the tetrahydrofolate-dependent step of the glycine cleavage reaction
-
r
S-aminomethyldihydrolipoylprotein + (6S)-tetrahydrofolate
dihydrolipoylprotein + (6R)-5,10-methylenetetrahydrofolate + NH3
show the reaction diagram
-
T-protein catalyzes the tetrahydrofolate-dependent step of the glycine cleavage reaction
-
?
S-aminomethyldihydrolipoylprotein + (6S)-tetrahydrofolate
dihydrolipoylprotein + (6R)-5,10-methylenetetrahydrofolate + NH3
show the reaction diagram
-
tetrahydrofolate-dependent enzyme
-
r
S-aminomethyldihydrolipoylprotein + (6S)-tetrahydrofolate
dihydrolipoylprotein + (6R)-5,10-methylenetetrahydrofolate + NH3
show the reaction diagram
-
tetrahydrofolate-dependent enzyme
-
?
S-aminomethyldihydrolipoylprotein + (6S)-tetrahydrofolate
dihydrolipoylprotein + (6R)-5,10-methylenetetrahydrofolate + NH3
show the reaction diagram
-
requires tetrahydrofolate
-
-
?
S-aminomethyldihydrolipoylprotein + (6S)-tetrahydrofolate
dihydrolipoylprotein + (6R)-5,10-methylenetetrahydrofolate + NH3
show the reaction diagram
-
folate-binding site: Lys-78, Lys-81 and Lys-352 are involved in binding, Lys-352 may serve as the primary binding site to alpha-carboxyl group of the first glutamate residue nearest the p-aminobenzoic acid ring of 5,10-methylenetetrahydrofolate and 5,10-methylenetetrahydropteroyltetraglutamate, Lys-81 may play a key role to hold the second glutamate residue through binding to its alpha-carboxyl group, 6.5fold higher affinity for 5,10-methylenetetrahydropteroyltetraglutamate than for 5,10-methylenetetrahydrofolate
-
r
S-aminomethyldihydrolipoylprotein + (6S)-tetrahydrofolate
dihydrolipoylprotein + (6R)-5,10-methylenetetrahydrofolate + NH3
show the reaction diagram
-
strictly dependent on tetrahydrofolate
-
r
S-aminomethyldihydrolipoylprotein + (6S)-tetrahydrofolate
dihydrolipoylprotein + (6R)-5,10-methylenetetrahydrofolate + NH3
show the reaction diagram
-
T-protein participates in the formation of the one carbon unit and ammonia or the reverse reaction
-
r
S-aminomethyldihydrolipoylprotein + (6S)-tetrahydrofolate
dihydrolipoylprotein + (6R)-5,10-methylenetetrahydrofolate + NH3
show the reaction diagram
-
important enzyme in glycine metabolism
-
-
?
S-aminomethyldihydrolipoylprotein + (6S)-tetrahydrofolate
dihydrolipoylprotein + (6R)-5,10-methylenetetrahydrofolate + NH3
show the reaction diagram
-
part of the glycine cleavage system
-
-
?
S-aminomethyldihydrolipoylprotein + (6S)-tetrahydrofolate
dihydrolipoylprotein + (6R)-5,10-methylenetetrahydrofolate + NH3
show the reaction diagram
-
part of the glycine cleavage system
-
-
?
S-aminomethyldihydrolipoylprotein + (6S)-tetrahydrofolate
dihydrolipoylprotein + (6R)-5,10-methylenetetrahydrofolate + NH3
show the reaction diagram
-
part of the glycine cleavage system
-
-
?
S-aminomethyldihydrolipoylprotein + (6S)-tetrahydrofolate
dihydrolipoylprotein + (6R)-5,10-methylenetetrahydrofolate + NH3
show the reaction diagram
-
glycine metabolism
-
-
?
S-aminomethyldihydrolipoylprotein + tetrahydropteroyltetraglutamate
dihydrolipoylprotein + 5,10-methylenetetrahydropteroyltetraglutamate + NH3
show the reaction diagram
-
-
better substrate than 5,10-methylenetetrahydrofolate, 6.5fold higher affinity for 5,10-methylenetetrahydropteroyltetraglutamate than for 5,10-methylenetetrahydrofolate
?
[protein]-S8-aminomethyldihydrolipoyllysine + tetrahydrofolate
[protein]-dihydrolipoyllysine + 5,10-methylenetetrahydrofolate + NH3
show the reaction diagram
-
-
-
-
r
additional information
?
-
-
component of the glycine cleavage system, T-protein is associated with H-protein forming a complex which is composed of one molecule of each of them
-
-
-
additional information
?
-
-
enzyme is a component of the glycine cleavage system which is composed of P-, H-, L- and T-protein, multienzyme complex
-
-
-
additional information
?
-
-
enzyme is a component of the glycine cleavage system which is composed of P-, H-, L- and T-protein, multienzyme complex
-
-
-
additional information
?
-
-
enzyme is a component of the glycine cleavage system which is composed of P-, H-, L- and T-protein, multienzyme complex
-
-
-
additional information
?
-
-
enzyme is a component of the glycine cleavage system which is composed of P-, H-, L- and T-protein, multienzyme complex
-
-
-
additional information
?
-
-
enzyme is a component of the reversible glycine cleavage system which is composed of 4 protein components named as P-, H-, L- and T-protein
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
S-aminomethyldihydrolipoylprotein + (6S)-tetrahydrofolate
dihydrolipoylprotein + (6R)-5,10-methylenetetrahydrofolate + NH3
show the reaction diagram
-
-
-
-
?
S-aminomethyldihydrolipoylprotein + (6S)-tetrahydrofolate
dihydrolipoylprotein + (6R)-5,10-methylenetetrahydrofolate + NH3
show the reaction diagram
-
important enzyme in glycine metabolism
-
-
?
S-aminomethyldihydrolipoylprotein + (6S)-tetrahydrofolate
dihydrolipoylprotein + (6R)-5,10-methylenetetrahydrofolate + NH3
show the reaction diagram
-
part of the glycine cleavage system
-
-
?
S-aminomethyldihydrolipoylprotein + (6S)-tetrahydrofolate
dihydrolipoylprotein + (6R)-5,10-methylenetetrahydrofolate + NH3
show the reaction diagram
-
part of the glycine cleavage system
-
-
?
S-aminomethyldihydrolipoylprotein + (6S)-tetrahydrofolate
dihydrolipoylprotein + (6R)-5,10-methylenetetrahydrofolate + NH3
show the reaction diagram
-
part of the glycine cleavage system
-
-
?
S-aminomethyldihydrolipoylprotein + (6S)-tetrahydrofolate
dihydrolipoylprotein + (6R)-5,10-methylenetetrahydrofolate + NH3
show the reaction diagram
-
glycine metabolism
-
-
?
[protein]-S8-aminomethyldihydrolipoyllysine + tetrahydrofolate
[protein]-dihydrolipoyllysine + 5,10-methylenetetrahydrofolate + NH3
show the reaction diagram
-
-
-
-
r
COFACTOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
pyridoxal 5'-phosphate
-
-
tetrahydrofolate
-
tetrahydrofolate-dependent enzyme
tetrahydrofolate
-
-
tetrahydrofolate
-
strictly dependent on tetrahydrofolate
tetrahydrofolate
-
requires tetrahydrofolate
tetrahydrofolate
-
folate-binding site; tetrahydrofolate-dependent enzyme
additional information
-
H-protein with reduced lipoate
-
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
iodoacetamide
-
5 mM, 70% inhibition
N-ethylmaleimide
-
0.1 mM, 70% inhibition
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.0677
-
5,10-methylenetetrahydrofolate
-
-
0.0869
-
5,10-methylenetetrahydrofolate
-
mutant T4A, His-tagged
0.0875
-
5,10-methylenetetrahydrofolate
-
mutant L6A, His-tagged
0.0881
-
5,10-methylenetetrahydrofolate
-
wild-type with His-tag
0.151
-
5,10-methylenetetrahydrofolate
-
N-terminal deletion mutant, His-tagged
0.0092
-
5,10-methylenetetrahydropteroyltetraglutamate
-
wild-type with His-tag
0.0104
-
5,10-methylenetetrahydropteroyltetraglutamate
-
-
0.0108
-
5,10-methylenetetrahydropteroyltetraglutamate
-
mutant L6A, His-tagged
0.0174
-
5,10-methylenetetrahydropteroyltetraglutamate
-
mutant T4A, His-tagged
65.4
-
NH4Cl
-
wild-type with His-tag
78.9
-
NH4Cl
-
mutant L6A, His-tagged
93.5
-
NH4Cl
-
mutant T4A, His-tagged
256
-
NH4Cl
-
N-terminal deletion mutant, His-tagged
0.00069
-
reduced H-protein
-
wild-type with His-tag
-
0.0012
-
reduced H-protein
-
mutant T4A, His-tagged
-
0.00237
-
reduced H-protein
-
mutant L6A, His-tagged
-
0.0169
-
reduced H-protein
-
N-terminal deletion mutant, His-tagged
-
0.0037
-
S-Aminomethyldihydrolipoylprotein
-
-
0.17
-
tetrahydrofolate
-
-
0.0382
-
5,10-methylenetetrahydropteroyltetraglutamate
-
N-terminal deletion mutant, His-tagged
additional information
-
additional information
-
values for mutant enzymes
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
2.1
-
5,10-methylenetetrahydrofolate
-
N-terminal deletion mutant, His-tagged
7.8
-
5,10-methylenetetrahydrofolate
-
mutant T4A, His-tagged
10.3
-
5,10-methylenetetrahydrofolate
-
mutant L6A, His-tagged
14.4
-
5,10-methylenetetrahydrofolate
-
-
18.4
-
5,10-methylenetetrahydrofolate
-
wild-type with His-tag
8.75
-
5,10-methylenetetrahydropteroyltetraglutamate
-
-
9.5
-
5,10-methylenetetrahydropteroyltetraglutamate
-
N-terminal deletion mutant, His-tagged
10.5
-
5,10-methylenetetrahydropteroyltetraglutamate
-
wild-type with His-tag
10.6
-
5,10-methylenetetrahydropteroyltetraglutamate
-
mutant L6A, His-tagged
3.9
-
NH4Cl
-
N-terminal deletion mutant, His-tagged
9.6
-
NH4Cl
-
mutant T4A, His-tagged
11.6
-
NH4Cl
-
mutant L6A, His-tagged
20.9
-
NH4Cl
-
wild-type with His-tag
2.9
-
reduced H-protein
-
N-terminal deletion mutant, His-tagged
-
8.5
-
reduced H-protein
-
mutant T4A, His-tagged
-
13.3
-
reduced H-protein
-
mutant L6A, His-tagged
-
19.4
-
reduced H-protein
-
wild-type with His-tag
-
11.6
-
5,10-methylenetetrahydropteroyltetraglutamate
-
mutant T4A, His-tagged
additional information
-
additional information
-
values for mutant enzymes
-
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
1.08
-
-
-
additional information
-
-
-
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
7
-
-
assay at
additional information
-
-
pI: 9.8
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
37
-
-
assay at
37
-
-
assay at
37
-
-
assay at
PDB
SCOP
CATH
ORGANISM
Bacillus subtilis (strain 168)
Bartonella henselae (strain ATCC 49882 / Houston 1)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
33000
-
-
gel filtration
37000
38000
-
sedimentation equilibrium centrifugation, gel filtration
45000
-
-
gel filtration
57000
-
-
T-protein in complex with H-protein, gel filtration
75000
-
-
dynamic light scattering
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 30000, SDS-PAGE
dimer
-
2 * 46170, calculated
dimer
-
crystallization data, cloverleaf-like orientation of protomer around a central hole
dimer
Pyrococcus horikoshii OT-3
-
2 * 46170, calculated; crystallization data, cloverleaf-like orientation of protomer around a central hole
-
monomer
-
1 * 45000, lithium dodecyl sulfate PAGE
monomer
-
1 * 41000, SDS-PAGE
monomer
-
conformational change after interaction with H-protein
monomer
-
-
monomer
-
conformational change after interaction with H-protein
additional information
-
construction of low-resolution model and tertiary structure model
additional information
-
interaction of enzyme with H-protein
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
aminomethyltransferase/T-protein in complex with dihydrolipoate-bearing H-protein and 5-methyltetrahydrofolate, a complex mimicking the ternary complex in the reverse reaction, purified recombinant wild-type and mutant T-proteins, hanging drop vapor diffusion method, mixing of 22-25 mg/ml proteins, T-protein and H protein, with an equal volume of reservoir solution containing 0.095 M 2-[4-(2-hydroxyethyl)-1-piperazinyl]ethanesulfonic acid, pH 7.5, 0.19 M calcium chloride, 26.6% v/v PEG 400, and 5% v/v glycerol, at 15C, 4-5 days to 2 weeks, soaking of the native crystals in mother liquid containing 1 mM (6S)-5-methyltetrahydrofolate at 15C for 4 h, X-ray diffraction structure determination and analysis at 2.0 A resolution, molecular replacement
-
apoform and bound to 5-methyltetrahydrofolate
P48728
apoform, tetrahydrofolate complex, folinic acid complex and lipoic acid complex of enzyme, homology model of human enzyme
-
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
50
-
-
1 min, 20% loss of activity
70
-
-
1 min, complete loss of activity
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
lability of enzyme under the conditions of its purifications and storage
-
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-20C, 20 mM Tris-HCl buffer, pH 8.0, 10 mM 2-mercaptoethanol, 50% v/v glycerol, at least 2 months, stable
-
-20C, 24 h, 60% loss of activity
-
0-4C, 1 week, stable
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
purification of recombinant enzyme, expressed in Escherichia coli BL21 (DE3)pLysS, and of mutants
-
641fold purification
-
8.8fold purification
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
C-terminally His6-tagged T-protein wild-type and mutant enzymes expression in Escherichia coli strain BL21(DE3)pLysS
-
Amt gene is located on chromosome 3p21 and contains 9 exons spanning about 6 kb of genomic sequence
-
transfection to Leishmania infantum and Leishmania major
-
cloning and sequencing of the Amt gene with 9 closely spaced exons that are contained within about 5 kb of genomic DNA, encoding a protein of 403 amino acids, cis-acting promoter is likely to be very short, Amt gene may be localized on chromosome 9F
-
EXPRESSION
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
decrease of expression of isogene 1 of T-protein component of glcycine cleavage complex in amastigote growth
-
response to heat stress in higher expression of isogene 1 of T-protein component of glcycine cleavage complex, inducible expression upon excess glycine
-
decrease of expression of isogene 1 of T-protein component of glcycine cleavage complex in amastigote growth
-
response to heat stress in higher expression of isogene 1 of T-protein component of glcycine cleavage complex, inducible expression upon excess glycine
-
increased expression upon exposure to light
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
D96N
-
site-directed mutagenesis, both the glycine cleavage and synthesis activities are reduced to 34% compared to the wild-type enzyme
D96N/Y188F
-
site-directed mutagenesis, the mutations abolish both the glycine cleavage and synthesis activities
D97N
-
site-directed mutagenesis, the mutation abolishes both the glycine cleavage and synthesis activities
D97N/Y188F
-
site-directed mutagenesis, the mutations abolish both the glycine cleavage and synthesis activities
K352E
-
mutant with 2fold increased Km-values for folate substrates
K352Q
-
mutant with 2fold increased Km-values for folate substrates
K352R
-
no effect on Km-values
K75E
-
mutant with 2.5fold increased Km-value for 5,10-methylenetetrahydrofolate and 8fold increased Km-value for 5,10-methylenetetrahydropteroyltetraglutamate
K78E
-
mutant with 1.4fold increased Km-values for folate substrates
K81E
-
mutant with 3fold increased Km-value for 5,10-methylenetetrahydrofolate and 16fold increased Km-value for 5,10-methylenetetrahydropteroyltetraglutamate
N113A
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site-directed mutagenesis, the mutation abolishes both the glycine cleavage and synthesis activities
N113A/R223A
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site-directed mutagenesis, the mutations abolish both the glycine cleavage and synthesis activities
N113D
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site-directed mutagenesis, the mutation abolishes both the glycine cleavage and synthesis activities
R223A
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site-directed mutagenesis, the mutation abolishes both the glycine cleavage and synthesis activities
R223K
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site-directed mutagenesis, the mutation abolishes both the glycine cleavage and synthesis activities
T4A
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2fold increase in Km-value for reduced H-protein
Y188F
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site-directed mutagenesis, both the glycine cleavage and synthesis activities are reduced to 83% compared to the wild-type enzyme
D276H
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nonketotic hyperglycinemia, rare mutation
E211K
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polymorphism occurring in patients with glycine encephalopathy, NKH, method for PCR-restriction enzyme analysis
G269D
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nonketotic hyperglycinemia, rare mutation
G47R
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nonketotic hyperglycinemia, rare mutation
N117I
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mutant may cause nonketotic hygerglycinemia
N145I
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nonketotic hyperglycinemia, substitution of conserved N, patient has servere neonatal presentation and died in the newborn period
Q192X
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nonketotic hyperglycinemia, premature stop codon
R296H
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mutation occurring in patients with glycine encephalopathy, NKH, method for PCR-restriction enzyme analysis
R318R
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polymorphism occurring in patients with glycine encephalopathy, NKH, method for PCR-restriction enzyme analysis
R320H
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allele frequency of 7% for R320H of T-protein in 50 patients with enzymatic confirmation of their diagnostics of nonketotic hyperglycinemia
L6A
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in contrast to wild-type, quite susceptible to trypsinolysis, 4fold increase in Km-value for reduced H-protein
additional information
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N-terminal deletion of 7 amino acids, in contrast to wild-type, quite susceptible to trypsinolysis
H42R
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present in many nonketotic hyperglycinemia affected members of an extended Israeli-Arab kindred
additional information
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allele frequency of 3% for T-protein splice site mutation IVS7-1G-A in 50 patients with enzymatic confirmation of their diagnostics of nonketotic hyperglycinemia, mutation with a one-base deletion 183delC
additional information
-
a subset of nonketotic hyperglycinemia cases is due to mutations in the gene for the T-protein
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
medicine
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strategy for molecular investigation of patients with nonketotic hyperglycinemia: defective glycine cleavage enzyme system, composed of P-, H-, T- and L-protein, 15% of patients have a T-protein defect
medicine
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a subset of nonketotic hyperglycinemia cases is due to mutations in the gene for the T-protein
medicine
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identification of several mutations and polymorphisms occurring in patients with glycine encephalopathy, NKH, and methods for their PCR-restriction enzyme analysis