Information on EC 2.6.1.16 - glutamine-fructose-6-phosphate transaminase (isomerizing)

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

EC NUMBER
COMMENTARY
2.6.1.16
-
RECOMMENDED NAME
GeneOntology No.
glutamine-fructose-6-phosphate transaminase (isomerizing)
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
L-glutamine + D-fructose 6-phosphate = L-glutamate + D-glucosamine 6-phosphate
show the reaction diagram
rapid equilibrium random mechanism
-
L-glutamine + D-fructose 6-phosphate = L-glutamate + D-glucosamine 6-phosphate
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
amino group transfer
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
Alanine, aspartate and glutamate metabolism
-
Amino sugar and nucleotide sugar metabolism
-
Biosynthesis of secondary metabolites
-
CMP-legionaminate biosynthesis I
-
Metabolic pathways
-
UDP-N-acetyl-D-glucosamine biosynthesis I
-
UDP-N-acetyl-D-glucosamine biosynthesis II
-
SYSTEMATIC NAME
IUBMB Comments
L-glutamine:D-fructose-6-phosphate isomerase (deaminating)
Although the overall reaction is that of a transferase, the mechanism involves the formation of ketimine between fructose 6-phosphate and a 6-amino group from a lysine residue at the active site, which is subsequently displaced by ammonia (transamidination).
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
2-amino-2-deoxy-D-glucose-6-phosphate ketol-isomerase
-
-
-
-
EC 5.3.1.19
-
-
formerly
-
GFAT
-
-
-
-
GFAT
-
-
GFAT
-
-
GFAT
Volvariella volvacea V1-1
Q6DLZ8
-
-
GFPT1
-
-
GlcN-6-P synthase
-
-
GlcN-6-P synthase
-
-
GlcN-6-P synthase
Q6DLZ8
-
GlcN-6-P synthase
Volvariella volvacea V1-1
Q6DLZ8
-
-
GlmS
-
in the absence of D-fructose 6-phosphate, the enzyme exhibits a weak hydrolyzing activity of Gln into Glu and ammonia (glutaminase activity), whereas the presence of D-fructose 6-phosphate strongly stimulates its hemisynthase activity
GlmS
P17169
-
glucosamine 6-phosphate synthase
-
-
-
-
glucosamine 6-phosphate synthetase
-
-
-
-
glucosamine phosphate isomerase (glutamine-forming)
-
-
-
-
glucosamine synthase
-
-
-
-
glucosamine synthase
-
-
glucosamine-6-P synthase
-
-
glucosamine-6-phosphate isomerase (glutamine-forming)
-
-
-
-
glucosamine-6-phosphate synthase
-
-
glucosamine-6-phosphate synthase
-
-
glucosamine-6-phosphate synthase
-
-
glucosamine-6-phosphate synthase
-
-
glucosamine-6-phosphate synthase
-
-
glucosamine-6-phosphate synthase
Q6DLZ8
-
glucosamine-6-phosphate synthase
Volvariella volvacea V1-1
Q6DLZ8
-
-
glucosamine-6-phosphate synthetase
-
-
-
-
glucosamine-6-phosphate synthetase
-
-
glucosamine-6P synthase
-
-
glucosamine:fructose-6-phosphate aminotransferase
-
-
-
-
glutamine-fructose 6-phosphate amidotransferase
-
-
-
-
glutamine-fructose 6-phosphate aminotransferase
-
-
-
-
glutamine-fructose-6-phosphate aminotransferase
-
-
glutamine: fructose-6-phosphate amidotransferase
-
-
glutamine: fructose-6-phosphate amidotransferase
-
-
glutamine: fructose-6-phosphate amidotransferase 1
-
-
glutamine: fructose-6-phosphate aminotransferase
-
-
glutamine:fructose-6-phosphate amidotransferase
-
-
glutamine:fructose-6-phosphate aminotransferase
-
-
-
-
hexosephosphate aminotransferase
-
-
-
-
isomerase, glucosamine phosphate (glutamine-forming)
-
-
-
-
L-glutamine D-fructose 6-phosphate amidotransferase
Q6DLZ8
-
L-glutamine D-fructose 6-phosphate amidotransferase
Volvariella volvacea V1-1
Q6DLZ8
-
-
L-glutamine fructose 6-phosphate transamidase
-
-
-
-
L-glutamine: D-fructose-6-phosphate amidotransferase
-
-
L-glutamine: L-fructose-6-phosphate amidotransferase
-
-
L-glutamine:D-fructose-6-phosphate amidotransferase
-
-
L-glutamine:D-fructose-6-phosphate amidotransferase (hexose isomerizing)
-
-
L-glutamine:D-fructose-6-phosphate amidotransferase (hexose-isomerizing)
Q6DLZ8
-
L-glutamine:D-fructose-6-phosphate amidotransferase (hexose-isomerizing)
Volvariella volvacea V1-1
Q6DLZ8
-
-
L-glutamine:L-fructose-6-phosphate amidotransferase
-
-
L-glutamine:L-fructose-6-phosphate amidotransferase
-
-
CAS REGISTRY NUMBER
COMMENTARY
9030-45-9
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
bovine
-
-
Manually annotated by BRENDA team
3000 Hfr strain (ATCC25257)
-
-
Manually annotated by BRENDA team
HB101 strain
-
-
Manually annotated by BRENDA team
strain HB101
-
-
Manually annotated by BRENDA team
strain HB101
UniProt
Manually annotated by BRENDA team
strain K-12
-
-
Manually annotated by BRENDA team
Helminthosporium sativum
-
-
-
Manually annotated by BRENDA team
glutamine:fructose-6-phosphate amidotransferase isoform 1
-
-
Manually annotated by BRENDA team
patients with type 2 diabetes
-
-
Manually annotated by BRENDA team
mouse
-
-
Manually annotated by BRENDA team
strain V1-1 (ATCC50447)
UniProt
Manually annotated by BRENDA team
Volvariella volvacea V1-1
strain V1-1 (ATCC50447)
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
physiological function
Q06210
glutamine:fructose-6-phosphate amidotransferase is a rate-limiting enzyme in the hexoamine biosynthetic pathway and plays an important role in type 2 diabetes
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
D-fructose 6-phosphate
D-glucose 6-phosphate
show the reaction diagram
-
isomerase activity studied over C-terminal D-fructose 6-phosphate binding domain constituted by residues 241 to 608
-
r
D-fructose 6-phosphate
D-glucose 6-phosphate
show the reaction diagram
-
determination of hexose phosphate-isomerizing activity
-
-
?
D-fructose 6-phosphate
D-glucose 6-phosphate
show the reaction diagram
-
determination of hexose phosphate-isomerizing activity
-
-
?
L-gamma-glutamyl-p-nitroanilide + D-fructose 6-phosphate
?
show the reaction diagram
-
-
-
-
?
L-gamma-glutamyl-p-nitroanilide + H2O
L-glutamine + p-nitroaniline
show the reaction diagram
-
determination of amidohydrolysing activity
-
-
?
L-gamma-glutamyl-p-nitroanilide + H2O
L-glutamine + p-nitroaniline
show the reaction diagram
-
determination of amidohydrolysing activity
-
-
?
L-gamma-glutamyl-p-nitroanilide + H2O
L-glutamine + p-nitroaniline
show the reaction diagram
-
determination of amidohydrolysing activity
-
-
?
L-glutamine + D-fructose 6-phosphate
L-glutamate + D-glucosamine 6-phosphate
show the reaction diagram
-
-
-
-
L-glutamine + D-fructose 6-phosphate
L-glutamate + D-glucosamine 6-phosphate
show the reaction diagram
-
-
-
-
L-glutamine + D-fructose 6-phosphate
L-glutamate + D-glucosamine 6-phosphate
show the reaction diagram
-
-
-
-
L-glutamine + D-fructose 6-phosphate
L-glutamate + D-glucosamine 6-phosphate
show the reaction diagram
-
-
-
-
L-glutamine + D-fructose 6-phosphate
L-glutamate + D-glucosamine 6-phosphate
show the reaction diagram
-
-
-
-
L-glutamine + D-fructose 6-phosphate
L-glutamate + D-glucosamine 6-phosphate
show the reaction diagram
-
-
-
-
?
L-glutamine + D-fructose 6-phosphate
L-glutamate + D-glucosamine 6-phosphate
show the reaction diagram
-
-
-
-
L-glutamine + D-fructose 6-phosphate
L-glutamate + D-glucosamine 6-phosphate
show the reaction diagram
-
-
-
-
L-glutamine + D-fructose 6-phosphate
L-glutamate + D-glucosamine 6-phosphate
show the reaction diagram
-
-
-
-
L-glutamine + D-fructose 6-phosphate
L-glutamate + D-glucosamine 6-phosphate
show the reaction diagram
-
-
-
?
L-glutamine + D-fructose 6-phosphate
L-glutamate + D-glucosamine 6-phosphate
show the reaction diagram
-
-
-
-
?
L-glutamine + D-fructose 6-phosphate
L-glutamate + D-glucosamine 6-phosphate
show the reaction diagram
P17169
-
-
-
?
L-glutamine + D-fructose 6-phosphate
L-glutamate + D-glucosamine 6-phosphate
show the reaction diagram
-
-
-
-
?
L-glutamine + D-fructose 6-phosphate
L-glutamate + D-glucosamine 6-phosphate
show the reaction diagram
-
-
-
ir
L-glutamine + D-fructose 6-phosphate
L-glutamate + D-glucosamine 6-phosphate
show the reaction diagram
-
-
-
-
L-glutamine + D-fructose 6-phosphate
L-glutamate + D-glucosamine 6-phosphate
show the reaction diagram
-
-
-
-
L-glutamine + D-fructose 6-phosphate
L-glutamate + D-glucosamine 6-phosphate
show the reaction diagram
-
-
-
-
?
L-glutamine + D-fructose 6-phosphate
L-glutamate + D-glucosamine 6-phosphate
show the reaction diagram
Q06210
-
-
-
?
L-glutamine + D-fructose 6-phosphate
L-glutamate + D-glucosamine 6-phosphate
show the reaction diagram
-
-
-
-
L-glutamine + D-fructose 6-phosphate
L-glutamate + D-glucosamine 6-phosphate
show the reaction diagram
-
-
-
-
L-glutamine + D-fructose 6-phosphate
L-glutamate + D-glucosamine 6-phosphate
show the reaction diagram
-
-
-
-
L-glutamine + D-fructose 6-phosphate
L-glutamate + D-glucosamine 6-phosphate
show the reaction diagram
-
-
-
-
L-glutamine + D-fructose 6-phosphate
L-glutamate + D-glucosamine 6-phosphate
show the reaction diagram
-
-
-
-
L-glutamine + D-fructose 6-phosphate
L-glutamate + D-glucosamine 6-phosphate
show the reaction diagram
-
-
-
-
L-glutamine + D-fructose 6-phosphate
L-glutamate + D-glucosamine 6-phosphate
show the reaction diagram
-
-
-
-
-
L-glutamine + D-fructose 6-phosphate
L-glutamate + D-glucosamine 6-phosphate
show the reaction diagram
-
-
-
?
L-glutamine + D-fructose 6-phosphate
L-glutamate + D-glucosamine 6-phosphate
show the reaction diagram
-
-
-
-
?
L-glutamine + D-fructose 6-phosphate
L-glutamate + D-glucosamine 6-phosphate
show the reaction diagram
-
-
-
-
L-glutamine + D-fructose 6-phosphate
L-glutamate + D-glucosamine 6-phosphate
show the reaction diagram
-
-
-
-
L-glutamine + D-fructose 6-phosphate
L-glutamate + D-glucosamine 6-phosphate
show the reaction diagram
-
-
-
-
L-glutamine + D-fructose 6-phosphate
L-glutamate + D-glucosamine 6-phosphate
show the reaction diagram
-
-
-
-
L-glutamine + D-fructose 6-phosphate
L-glutamate + D-glucosamine 6-phosphate
show the reaction diagram
-
-
-
-
L-glutamine + D-fructose 6-phosphate
L-glutamate + D-glucosamine 6-phosphate
show the reaction diagram
-
-
-
-
?
L-glutamine + D-fructose 6-phosphate
L-glutamate + D-glucosamine 6-phosphate
show the reaction diagram
-
-
-
-
ir
L-glutamine + D-fructose 6-phosphate
L-glutamate + D-glucosamine 6-phosphate
show the reaction diagram
-
-
-
-
L-glutamine + D-fructose 6-phosphate
L-glutamate + D-glucosamine 6-phosphate
show the reaction diagram
-
-
-
-
L-glutamine + D-fructose 6-phosphate
L-glutamate + D-glucosamine 6-phosphate
show the reaction diagram
-
-
-
-
L-glutamine + D-fructose 6-phosphate
L-glutamate + D-glucosamine 6-phosphate
show the reaction diagram
-
-
-
-
L-glutamine + D-fructose 6-phosphate
L-glutamate + D-glucosamine 6-phosphate
show the reaction diagram
Helminthosporium sativum, Neurospora tetrasperma
-
-
-
-
L-glutamine + D-fructose 6-phosphate
L-glutamate + D-glucosamine 6-phosphate
show the reaction diagram
-
-
-
-
ir
L-glutamine + D-fructose 6-phosphate
L-glutamate + D-glucosamine 6-phosphate
show the reaction diagram
-, Q8G545
-
-
-
?
L-glutamine + D-fructose 6-phosphate
L-glutamate + D-glucosamine 6-phosphate
show the reaction diagram
-
-
-
-
?
L-glutamine + D-fructose 6-phosphate
L-glutamate + D-glucosamine 6-phosphate
show the reaction diagram
Q6DLZ8
-
-
-
?
L-glutamine + D-fructose 6-phosphate
L-glutamate + D-glucosamine 6-phosphate
show the reaction diagram
-
specific for: L-glutamine
-
-
L-glutamine + D-fructose 6-phosphate
L-glutamate + D-glucosamine 6-phosphate
show the reaction diagram
-
specific for: L-glutamine
-
ir
L-glutamine + D-fructose 6-phosphate
L-glutamate + D-glucosamine 6-phosphate
show the reaction diagram
-
specific for: L-glutamine
-
-
L-glutamine + D-fructose 6-phosphate
L-glutamate + D-glucosamine 6-phosphate
show the reaction diagram
-
specific for: L-glutamine
-
ir
L-glutamine + D-fructose 6-phosphate
L-glutamate + D-glucosamine 6-phosphate
show the reaction diagram
P17169
mechanism proposed
-
-
-
L-glutamine + D-fructose 6-phosphate
L-glutamate + D-glucosamine 6-phosphate
show the reaction diagram
-
importance for N-acetylglucosamine synthesis in human liver
-
?
L-glutamine + D-fructose 6-phosphate
L-glutamate + D-glucosamine 6-phosphate
show the reaction diagram
-
enzyme plays a key role in induction of insulin resistance in cultured cells
-
?
L-glutamine + D-fructose 6-phosphate
L-glutamate + D-glucosamine 6-phosphate
show the reaction diagram
Volvariella volvacea V1-1
Q6DLZ8
-
-
-
?
additional information
?
-
-
asparagine is not a substrate
-
-
-
additional information
?
-
-, Q8G545
enzyme possesses an independent glutaminase activity, converting glutamine to glutamate in the absence of fructose 6-phosphate
-
-
-
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
L-glutamine + D-fructose 6-phosphate
L-glutamate + D-glucosamine 6-phosphate
show the reaction diagram
-
-
-
?
L-glutamine + D-fructose 6-phosphate
L-glutamate + D-glucosamine 6-phosphate
show the reaction diagram
Q06210
-
-
-
?
L-glutamine + D-fructose 6-phosphate
L-glutamate + D-glucosamine 6-phosphate
show the reaction diagram
-
-
-
?
L-glutamine + D-fructose 6-phosphate
L-glutamate + D-glucosamine 6-phosphate
show the reaction diagram
-
importance for N-acetylglucosamine synthesis in human liver
-
?
L-glutamine + D-fructose 6-phosphate
L-glutamate + D-glucosamine 6-phosphate
show the reaction diagram
-
enzyme plays a key role in induction of insulin resistance in cultured cells
-
?
COFACTOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
additional information
-
no cofactor requirement
-
additional information
-
-
-
additional information
-
glmS ribozyme employs a small-molecule cofactor. Binding of D-glucosamine 6-phosphate (GlcN6P) uncovers the latent self-cleavage activity of the RNA, which adopts a catalytically competent conformation that is nonetheless inactive in the absence of GlcN6P
-
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
(2S)-2-amino-3-(([(2R,3R)-3-benzoyloxiran-2-yl]carbonyl)amino)propanoic acid
-
-
-
(2S)-2-amino-3-([(2E)-4-oxo-4-phenylbut-2-enoyl]amino)propanoic acid
-
-
-
(2S)-2-amino-3-([(2E)-4-oxopent-2-enoyl]amino)propanoic acid
-
-
-
(2S)-3-(([(2R,3R)-3-acetyloxiran-2-yl]carbonyl)amino)-2-aminopropanoic acid
-
-
-
1,1'-dithiodiformamidine
-
irreversible inhibition
1,2-anhydrohexitol 6-phosphate
-
mixture of the four diastereoisomers. Irreversible inactivation. D-fructose 6-phosphate and 2-amino-2-deoxyglucitol protect, L-glutamine does not
2-amino-2-deoxy-D-glucitol 6-phosphate
-
-
2-amino-2-deoxy-D-glucitol 6-phosphate
-
-
2-amino-2-deoxy-D-glucitol-6-phosphate
-
inhibitor of the sugar isomerising domain
2-amino-2-deoxy-D-glucitol-6-phosphate
-
-
2-amino-2-deoxy-D-glucitol-6-phosphate
-
IC50: 0.056 mM
2-amino-2-deoxy-D-glucitol-6-phosphate
Q6DLZ8
-
2-amino-2-deoxy-D-glucitol-6-phosphate dimethyl ester
-
-
2-amino-2-deoxy-D-mannitol 6-phosphate
-
-
2-amino-2-deoxy-D-mannitol-6-phosphate
-
exhibits stronger affinity for the sugar-binding site of GlcN-6-P synthase than 2-amino-2-deoxy-D-glucitol-6-phosphate
2-amino-2-deoxy-D-mannitol-6-phosphate
-
-
2-Amino-2-deoxyglucitol 6-phosphate
-
competitive with respect to D-fructose 6-phosphate
4,4'-dithiodipyridine
-
inactivation reversed by dithiothreitol. Competitive with respect to L-glutamine. Non-competitive with respect to D-fructose 6-phosphate
4-(furan-2-ylcarbonyl)-3-hydroxy-5-(4-phenoxyphenyl)-1-(pyridin-3-ylmethyl)-1,5-dihydro-2H-pyrrol-2-one
-
20% inhibition at 0.1 mM
5,5'-dithionitrobenzoic acid
-
irreversible inhibition
-
5,5'-dithionitrobenzoic acid
-
irreversible inhibition
-
5,5'-dithionitrobenzoic acid
-
inactivation reversed by dithiothreitol
-
5-phospho-D-arabinoamide
-
-
6,6'-Dithiodinicotinic acid
-
irreversible inhibition
6,7-bis(2-methoxyphenyl)-10-methyl-1,4,7,12-tetrahydro-6H-chromeno[4,3-d][1,2,4]triazolo[1,5-a]pyrimidine
-
70% inhibition at 0.1 mM
6-diazo-5-oxo-L-norleucine
-
-
6-diazo-5-oxo-L-norleucine
-
competitive with respect to L-glutamine
6-diazo-5-oxo-L-norleucine
-
-
6-diazo-5-oxo-L-norleucine
-
-
6-diazo-5-oxo-L-norleucine
-
inhibitor of the glutamine binding site
6-diazo-5-oxo-L-norleucine
P17169
2 mM
6-diazo-5-oxo-L-norleucine
-
-
Aaptamine
-
IC50: 0.12 mM
amitrole
-
IC50: 0.1 mM
Anticapsin
-
L-glutamine protects, irreversible inhibition
Anticapsin
-
competitive
Anticapsin
-
inhibitor of the glutamine binding site
arabinose oxime 5-phosphate
-
inhibitor of the sugar isomerising domain
azaserine
-
weak
azaserine
-
weak
D-glucitol 6-phosphate
-
competitive with respect to D-fructose 6-phosphate
D-Glucosamine 6-phosphate
-
negative feedback-regulation at post-transcriptional level. The biological function of small RNA GlmZ is to positively control the enzyme's mRNA in response to D-glucosamine 6-phosphate concentrations. YhbJ, a gene of the rpoN operon, negatively regulates GlmZ
D-Glucosamine-6-phosphate
-
1 mM, about 50% loss of activity
Dihydroxyacetone
-
weak
dihydroxyacetone phosphate
-
weak
DL-delta-1-pyrroline-5-carboxylate
-
competitive with respect to L-glutamine
ethyl 2-[2-(3-bromophenyl)-3-[(4-fluorophenyl)carbonyl]-4-hydroxy-5-oxo-2,5-dihydro-1H-pyrrol 1-yl]-4-methyl-1,3-thiazole-5-carboxylate
-
70% inhibition at 0.1 mM
ethyl 2-[3-[(4-fluorophenyl)carbonyl]-4-hydroxy-2-(4-methoxyphenyl)-5-oxo-2,5-dihydro-1H pyrrol-1-yl]-4-methyl-1,3-thiazole-5-carboxylate
-
70% inhibition at 0.1 mM
fructose 1,6-diphosphate
-
weak
glyceraldehyde 3-phosphate
-
50% inhibition at 0.2 mM
glycolaldehyde
-
weak
Glyoxal
-
50% inhibition at 0.03 mM
iodoacetamide
-
-
L-alpha-glycerophosphate
-
weak
Mercuric chloride
-
84% inhibition at 1 mM
Methylglyoxal
-
50% inhibition at 0.01 mM, non competitive
N-acetyl-2-amino-2-deoxy-D-glucitol-6-phosphate
-
-
N-ethylmaleimide
-
irreversible inhibition
N-ethylmaleimide
-
78% inhibition at1 mM
N-iodoacetylglucosamine 6-phosphate
-
D-fructose 6-phosphate protects
N3-(4-Methoxyfumaroyl)-L-2,3-diaminopropanoic acid
-
L-glutamine and some analogs protect
N3-(4-Methoxyfumaroyl)-L-2,3-diaminopropanoic acid
-
-
N3-(4-Methoxyfumaroyl)-L-2,3-diaminopropanoic acid
-
acts as active-site-directed inactivator blocking the N-terminal, glutamine-binding domain of the enzyme; inhibitor of the glutamine binding site
N3-(4-Methoxyfumaroyl)-L-2,3-diaminopropanoic acid
Q6DLZ8
-
N3-bromoacetyl-L-2,3-diaminopropanoic acid
-
competitive with respect to L-glutamine
N3-bromoacetyl-L-2,3-diaminopropanoic acid
-
inhibitor of the glutamine binding site
N3-chloroacetyl-L-2,3-diaminopropanoic acid
-
competitive with respect to L-glutamine
N3-fumaramoyl-L-2,3-diaminopropanoic acid
-
-
N3-fumaramoyl-L-2,3-diaminopropanoic acid
-
-
N3-Fumaroyl-L-2,3-diaminopropanoic acid
-
-
N3-Fumaroyl-L-2,3-diaminopropanoic acid
-
-
N3-Fumaroylcarboxyamido-L-2,3-diaminopropionic acid
-
competitive with L-glutamine
-
N3-Fumaroylcarboxyamido-L-2,3-diaminopropionic acid
-
-
-
N3-iodoacetyl-L-2,3-diaminopropanoic acid
-
competitive with respect to L-glutamine
N3-L-trans-epoxysuccinamoyl-L-2,3-diaminopropanoic acid
-
inhibitor of the glutamine binding site
N4-(4-Methoxyfumaroyl)-L-2,4-diaminobutanoic acid
-
-
p-chloromercuribenzoate
-
-
p-chloromercuribenzoate
-
84% inhibition at 0.1 mM
pyridoxamine-5'-phosphate
-
-
Tolbutamide
-
80% inhibition at 2 mg/ml
UDP-glucose
-
-
UDP-N-acetyl-alpha-D-glucosamine
-
-
UDP-N-acetylglucosamine
-
competitive with respect to D-fructose 6-phosphate, non-competitive with respect to L-glutamine
UDP-N-acetylglucosamine
-
weak
UDP-N-acetylglucosamine
-
partial
UDP-N-acetylglucosamine
-
40% inhibition at 1 mM
UDP-N-acetylglucosamine
-
competitive inhibitor with respect to D-fructose 6-phosphate
UDP-N-acetylglucosamine
-
feed-back inhibition
UDP-N-acetylglucosamine
-
-
uridine 5'-diphospho-N-acetyl-D-glucosamine
-
-
-
uridine 5'-diphospho-N-acetylglucosamine
Q6DLZ8
-
Methylglyoxal
-
inhibits preincubated enzyme less profoundly than the untreated enzyme
additional information
-
no inhibition by 0.1 mM c3, 4, 6, 9, 12, 13
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
chondroitin sulfate B
-
-
Desferrioxamine
-
0.2 mM; activation of gene expression via iron chelation
Picolinic acid
-
2 mM; activation of gene expression via iron chelation
dithiothreitol
-
1 mM, activates 1.8fold
additional information
-
small acidic compound devoid of SH groups thermolabile at 100C dialyzable, not precipitable with HClO4 easily separated from proteins in a Sephadex G-25 column
-
additional information
-
requires methionine aminopeptidase activity for proper function
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.2
-
D-fructose 6-phosphate
-
wild type enzyme
0.23
-
D-fructose 6-phosphate
-
calorimetric determination, pH 7.2, 37C
0.25
-
D-fructose 6-phosphate
-
pH 7.5, 37C
0.3
-
D-fructose 6-phosphate
-
calorimetric determination, pH 7.2, 25C
0.36
-
D-fructose 6-phosphate
-
wild-type, 37C; wild type enzyme, in 50 mM potassium phosphate, pH 7.5, 1 mM EDTA, 50 mM KCl, at 37C
0.38
-
D-fructose 6-phosphate
-
pH 7.7, 37C
0.39
-
D-fructose 6-phosphate
-
pH 7.0, 37C
0.4
-
D-fructose 6-phosphate
-
-
0.5
-
D-fructose 6-phosphate
-
pH 6.3, 38C
0.52
-
D-fructose 6-phosphate
-
mutant S243E, 37C, pH 7.5
0.55
-
D-fructose 6-phosphate
Q6DLZ8
recombinant enzyme, in 10 mM KCl, 1 mg/ml bovine serum albumin, 20 mM imidazole buffer (pH 6.8), 1 mM EDTA, 1 mM dithiothreitol, and 10% (v/v) glycerol
0.67
-
D-fructose 6-phosphate
-
mutant enzyme V605L, in 50 mM potassium phosphate, pH 7.5, 1 mM EDTA, 50 mM KCl, at 37C; mutant V605L, 37C
0.75
-
D-fructose 6-phosphate
-
pH 7.0, 37C
0.93
-
D-fructose 6-phosphate
-
mutant enzyme W74A, in 50 mM potassium phosphate, pH 7.5, 1 mM EDTA, 50 mM KCl, at 37C; mutant W74A, 37C
1.04
-
D-fructose 6-phosphate
-
wild-type, 37C, pH 7.5
1.08
-
D-fructose 6-phosphate
-
hexose phosphate-isomerizing activity, wild-type with N-terminal His-tag, pH 7.5, 25C
1.11
-
D-fructose 6-phosphate
-
mutant enzyme W74L, in 50 mM potassium phosphate, pH 7.5, 1 mM EDTA, 50 mM KCl, at 37C; mutant W74L, 37C
1.12
-
D-fructose 6-phosphate
-
mutant mutant Gfa1-His6DELTA655-660, pH 6.8, 37C
1.15
-
D-fructose 6-phosphate
-
mutant A602L, 37C; mutant enzyme A602L, in 50 mM potassium phosphate, pH 7.5, 1 mM EDTA, 50 mM KCl, at 37C
1.2
-
D-fructose 6-phosphate
-
hexose phosphate-isomerizing activity, wild-type, pH 7.5, 25C; reaction mixture contains 2 mM D-fructose 6-phosphate, 0.5 mM NADP+, 1 mM EDTA, and appropriately diluted GlcN-6-P synthase preparation in 50 mM Tris/HCl buffer (pH 7.5) at 25C
1.2
-
D-fructose 6-phosphate
-
wild type enzyme, in in 25 mM potassium phosphate buffer at pH 7.0 and 37C
1.4
-
D-fructose 6-phosphate
-
hexose phosphate-isomerizing activity, residues 346-712, His-tagged hexose phosphate-isomerizing domain, pH 7.5, 25C
1.41
-
D-fructose 6-phosphate
-
glutamine 6-phosphate-synthetic activity, wild-type, pH 7.5, 25C
1.45
-
D-fructose 6-phosphate
-
mutant enzyme W74F, in 50 mM potassium phosphate, pH 7.5, 1 mM EDTA, 50 mM KCl, at 37C; mutant W74F, 37C
1.56
-
D-fructose 6-phosphate
-
wild-type, pH 6.8, 37C
1.9
-
D-fructose 6-phosphate
-
mutant mutant Gfa1-K568H/S569H, pH 6.8, 37C
2
-
D-fructose 6-phosphate
-
pH 7.0, 37C
2
-
D-fructose 6-phosphate
-
pH 7.5, 37C
2.6
-
D-fructose 6-phosphate
-
mutant Gfa1-His6DELTA343-348, pH 6.8, 37C
3.8
-
D-fructose 6-phosphate
-
pH 6.5, 30C
3.8
-
D-fructose 6-phosphate
-
pH 7.2, 37C, isomerization catalyzed by C-terminal domain
6.5
-
D-fructose 6-phosphate
-
hexose phosphate-isomerizing activity, wild-type with C-terminal His-tag, pH 7.5, 25C
16
-
D-glucose 6-phosphate
-
pH 7.2, 37C, isomerization catalyzed by C-terminal domain
1
-
glutamine
-
-
0.67
-
L-gamma -glutamyl-p-nitroanilide
-
reaction mixture contains 1 mM L-gamma-glutamyl-p-nitroanilide, 1 mM EDTA, 1 mM DTT and the appropriately diluted enzyme preparation in 20 mM HEPES buffer (pH 7.5) at 25C
0.0064
-
L-gamma-glutamyl-p-nitroanilide
-
mutant W74F, 37C
0.05
-
L-gamma-glutamyl-p-nitroanilide
-
wild-type, 37C
0.1
-
L-gamma-glutamyl-p-nitroanilide
-
mutant W74L, 37C
0.2
-
L-gamma-glutamyl-p-nitroanilide
-
mutant W74A, 37C
0.29
-
L-gamma-glutamyl-p-nitroanilide
-
mutant V605L, 37C
0.31
-
L-gamma-glutamyl-p-nitroanilide
-
residues 1-345, His-tagged glutamine amide-hydrolysing domain, pH 7.5, 25C
0.36
-
L-gamma-glutamyl-p-nitroanilide
-
mutant A602L, 37C
0.64
-
L-gamma-glutamyl-p-nitroanilide
-
wild-type with C-terminal His-tag, pH 7.5, 25C
0.67
-
L-gamma-glutamyl-p-nitroanilide
-
wild-type, pH 7.5, 25C
1.8
-
L-gamma-glutamyl-p-nitroanilide
-
both wild-type and mutant S243E, 37C, pH 7.5
12.2
-
L-gamma-glutamyl-p-nitroanilide
-
wild-type with N-terminal His-tag, pH 7.5, 25C
0.2
-
L-glutamate
-
calorimetric determination, pH 7.2, 25C
0.34
-
L-glutamate
-
reaction mixture contains 10 mM L-glutamate, 1 mM EDTA, 1 mM DTT and an appropriately diluted enzyme preparation in 20 mM HEPES buffer (pH 7.5) at 25C
1.33
-
L-glutamate
-
mutant Gfa1-K568H/S569H, pH 6.8, 37C
1.36
-
L-glutamate
-
mutant Gfa1-His6DELTA343-348, pH 6.8, 37C
1.41
-
L-glutamate
-
wild-type, pH 6.8, 37C
2.36
-
L-glutamate
-
mutant Gfa1-His6DELTA655-660, pH 6.8, 37C
0.04
-
L-glutamine
-
mutant enzyme W74L, in 50 mM potassium phosphate, pH 7.5, 1 mM EDTA, 50 mM KCl, at 37C; mutant W74L, 37C
0.048
-
L-glutamine
-
mutant enzyme W74F, in 50 mM potassium phosphate, pH 7.5, 1 mM EDTA, 50 mM KCl, at 37C; mutant W74F, 37C
0.072
-
L-glutamine
-
mutant enzyme V605L, in 50 mM potassium phosphate, pH 7.5, 1 mM EDTA, 50 mM KCl, at 37C; mutant V605L, 37C
0.1
-
L-glutamine
-
mutant A602L, 37C; mutant enzyme A602L, in 50 mM potassium phosphate, pH 7.5, 1 mM EDTA, 50 mM KCl, at 37C
0.17
-
L-glutamine
-
wild type enzyme
0.2
-
L-glutamine
-
pH 7.4, 37C
0.2
-
L-glutamine
-
pH 7.5, 37C
0.225
-
L-glutamine
-
pH 7.5, 37C
0.27
-
L-glutamine
-
wild-type, 37C; wild type enzyme, in 50 mM potassium phosphate, pH 7.5, 1 mM EDTA, 50 mM KCl, at 37C
0.3
-
L-glutamine
-
pH 6.3, 38C
0.34
-
L-glutamine
-
glutamine 6-phosphate-synthetic activity, wild-type, pH 7.5, 25C
0.38
-
L-glutamine
-
mutant enzyme W74A, in 50 mM potassium phosphate, pH 7.5, 1 mM EDTA, 50 mM KCl, at 37C; mutant W74A, 37C
0.4
-
L-glutamine
-
pH 7.5, 37C
0.5
-
L-glutamine
-
pH 6.5, 30C
0.6
-
L-glutamine
-
pH 7.5, 37C
0.65
-
L-glutamine
-
pH 7.0, 37C
0.74
-
L-glutamine
-
pH 7.0, 37C
0.75
-
L-glutamine
Q6DLZ8
recombinant enzyme, in 10 mM KCl, 1 mg/ml bovine serum albumin, 20 mM imidazole buffer (pH 6.8), 1 mM EDTA, 1 mM dithiothreitol, and 10% (v/v) glycerol
0.8
-
L-glutamine
-
-
0.85
-
L-glutamine
-
pH 7.5, 37C
1.6
-
L-glutamine
-
pH 7.7, 37C
5.1
-
L-glutamine
-, Q8G545
pH 7.0, 55C
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.004
-
D-fructose 6-phosphate
-
hexose phosphate-isomerizing activity, wild-type with C-terminal His-tag, pH 7.5, 25C
0.0092
-
D-fructose 6-phosphate
-
hexose phosphate-isomerizing activity, residues 346-712, His-tagged hexose phosphate-isomerizing domain, pH 7.5, 25C
0.021
-
D-fructose 6-phosphate
-
hexose phosphate-isomerizing activity, wild-type, pH 7.5, 25C; hexose phosphate-isomerizing activity, wild-type with N-terminal His-tag, pH 7.5, 25C
0.0213
-
D-fructose 6-phosphate
-
reaction mixture contains 2 mM D-fructose 6-phosphate, 0.5 mM NADP+, 1 mM EDTA, and appropriately diluted GlcN-6-P synthase preparation in 50 mM Tris/HCl buffer (pH 7.5) at 25C
0.08
-
D-fructose 6-phosphate
-
mutant W74L, 37C
0.083
-
D-fructose 6-phosphate
-
mutant enzyme W74L, in 50 mM potassium phosphate, pH 7.5, 1 mM EDTA, 50 mM KCl, at 37C
0.12
-
D-fructose 6-phosphate
-
mutant enzyme W74A, in 50 mM potassium phosphate, pH 7.5, 1 mM EDTA, 50 mM KCl, at 37C; mutant W74A, 37C
0.15
-
D-fructose 6-phosphate
-
mutant enzyme V605L, in 50 mM potassium phosphate, pH 7.5, 1 mM EDTA, 50 mM KCl, at 37C; mutant V605L, 37C
0.22
-
D-fructose 6-phosphate
-
mutant A602L, 37C; mutant enzyme A602L, in 50 mM potassium phosphate, pH 7.5, 1 mM EDTA, 50 mM KCl, at 37C
0.52
-
D-fructose 6-phosphate
-
wild type enzyme, in 50 mM potassium phosphate, pH 7.5, 1 mM EDTA, 50 mM KCl, at 37C
0.92
-
D-fructose 6-phosphate
-
mutant enzyme W74F, in 50 mM potassium phosphate, pH 7.5, 1 mM EDTA, 50 mM KCl, at 37C; mutant W74F, 37C
9.9
-
D-fructose 6-phosphate
-
calorimetric determination, pH 7.2, 25C
12
-
D-fructose 6-phosphate
-
calorimetric determination, pH 7.2, 37C
14.4
-
D-fructose 6-phosphate
-
wild-type, 37C
14.42
-
D-fructose 6-phosphate
-
wild type enzyme, in 50 mM potassium phosphate, pH 7.5, 1 mM EDTA, 50 mM KCl, at 37C
35.5
-
D-fructose 6-phosphate
-
co-substrate: L-glutamine, pH 7.0, 37C
0.00092
-
L-gamma-glutamyl-p-nitroanilide
-
wild-type with N-terminal His-tag, pH 7.5, 25C
0.0075
-
L-gamma-glutamyl-p-nitroanilide
-
residues 1-345, His-tagged glutamine amide-hydrolysing domain, pH 7.5, 25C
0.012
-
L-gamma-glutamyl-p-nitroanilide
-
wild-type, pH 7.5, 25C
0.0123
-
L-gamma-glutamyl-p-nitroanilide
-
reaction mixture contains 1 mM L-gamma-glutamyl-p-nitroanilide, 1 mM EDTA, 1 mM DTT and the appropriately diluted enzyme preparation in 20 mM HEPES buffer (pH 7.5) at 25C
0.013
-
L-gamma-glutamyl-p-nitroanilide
-
wild-type with C-terminal His-tag, pH 7.5, 25C
0.13
-
L-gamma-glutamyl-p-nitroanilide
-
mutant V605L, 37C
0.15
-
L-gamma-glutamyl-p-nitroanilide
-
mutant A602L, 37C
0.17
-
L-gamma-glutamyl-p-nitroanilide
-
wild-type, 37C
0.5
-
L-gamma-glutamyl-p-nitroanilide
-
mutant W74L, 37C
0.67
-
L-gamma-glutamyl-p-nitroanilide
-
mutant W74F, 37C
0.68
-
L-gamma-glutamyl-p-nitroanilide
-
mutant W74A, 37C
9.81
-
L-glutamate
-
calorimetric determination, pH 7.2, 25C
12
-
L-glutamate
-
reaction mixture contains 10 mM L-glutamate, 1 mM EDTA, 1 mM DTT and an appropriately diluted enzyme preparation in 20 mM HEPES buffer (pH 7.5) at 25C
0.28
-
L-glutamine
-
mutant enzyme V605L, in 50 mM potassium phosphate, pH 7.5, 1 mM EDTA, 50 mM KCl, at 37C; mutant V605L, 37C
0.38
-
L-glutamine
-
mutant A602L, 37C; mutant enzyme A602L, in 50 mM potassium phosphate, pH 7.5, 1 mM EDTA, 50 mM KCl, at 37C
0.97
-
L-glutamine
-
wild type enzyme, in 50 mM potassium phosphate, pH 7.5, 1 mM EDTA, 50 mM KCl, at 37C
1.5
-
L-glutamine
-
mutant W74L, 37C
1.55
-
L-glutamine
-
mutant enzyme W74L, in 50 mM potassium phosphate, pH 7.5, 1 mM EDTA, 50 mM KCl, at 37C
3
-
L-glutamine
-
mutant W74A, 37C
3.02
-
L-glutamine
-
mutant enzyme W74A, in 50 mM potassium phosphate, pH 7.5, 1 mM EDTA, 50 mM KCl, at 37C
7.17
-
L-glutamine
-
mutant enzyme W74F, in 50 mM potassium phosphate, pH 7.5, 1 mM EDTA, 50 mM KCl, at 37C
7.2
-
L-glutamine
-
mutant W74F, 37C
12
-
L-glutamine
-
glutamine 6-phosphate-synthetic activity, wild-type, pH 7.5, 25C
17.17
-
L-glutamine
-
wild type enzyme, in 50 mM potassium phosphate, pH 7.5, 1 mM EDTA, 50 mM KCl, at 37C
17.2
-
L-glutamine
-
wild-type, 37C
35.5
-
L-glutamine
-
co-substrate: D-fructose 6-phosphate, pH 7.0, 37C
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.45
-
(2S)-2-amino-3-(([(2R,3R)-3-benzoyloxiran-2-yl]carbonyl)amino)propanoic acid
-
pH 7.0, 37C
-
0.056
-
(2S)-2-amino-3-([(2E)-4-oxo-4-phenylbut-2-enoyl]amino)propanoic acid
-
pH 7.0, 37C
-
15.2
-
(2S)-2-amino-3-([(2E)-4-oxopent-2-enoyl]amino)propanoic acid
-
pH 7.0, 37C
-
19.4
-
(2S)-3-(([(2R,3R)-3-acetyloxiran-2-yl]carbonyl)amino)-2-aminopropanoic acid
-
pH 7.0, 37C
-
0.018
-
2-amino-2-deoxy-D-glucitol 6-phosphate
-
pH 7.5, 37C
0.035
-
2-amino-2-deoxy-D-glucitol-6-phosphate
-
-
0.68
-
2-amino-2-deoxy-D-glucitol-6-phosphate dimethyl ester
-
-
0.00067
-
2-amino-2-deoxy-D-mannitol 6-phosphate
-
pH 7.5, 37C
0.009
-
2-amino-2-deoxy-D-mannitol-6-phosphate
-
-
0.0193
-
2-Amino-2-deoxyglucitol 6-phosphate
-
pH 7.5, 25C
0.088
-
2-Amino-2-deoxyglucitol 6-phosphate
-
takes into account 2.2% of the open form present in a solution of D-fructose 6-phosphate
0.095
-
4-Glutamylhydroxamate
-
pH 7.5, 37C
0.62
-
5-phospho-D-arabinoamide
-
-
0.001
-
6-diazo-5-oxo-L-norleucine
-
pH 7.4, 37C
0.0014
-
6-diazo-5-oxo-L-norleucine
-
pH 7.5, 37C
0.0025
-
6-diazo-5-oxo-L-norleucine
-
-
0.0028
-
6-diazo-5-oxo-L-norleucine
-
pH 7.5, room temperature
0.0075
-
6-diazo-5-oxo-L-norleucine
-
pH 7.5, 37C
0.00011
-
Anticapsin
-
pH 7.5, 37C
0.00053
-
Anticapsin
-
pH 7.5, 37C
0.00056
-
Anticapsin
-
pH 7.5, 37C
0.00075
-
Anticapsin
-
pH 7.5, 37C
2.46
-
D-glucitol 6-phosphate
-
pH 7.2
0.023
-
DL-delta-1-pyrroline-5-carboxylate
-
-
0.56
-
Glucosamine-6-phosphate
-
wild type enzyme
12.6
-
iodoacetamide
-
pH 7.5, room temperature
0.84
-
N-acetyl-2-amino-2-deoxy-D-glucitol-6-phosphate
-
-
0.00027
-
N3-(4-Methoxyfumaroyl)-L-2,3-diaminopropanoic acid
-
pH 7.5, 37C
0.00035
-
N3-(4-Methoxyfumaroyl)-L-2,3-diaminopropanoic acid
-
pH 7.5, 37C
0.0001
-
N3-bromoacetyl-L-2,3-diaminopropanoic acid
-
pH 6.5, 25C
0.0006
-
N3-chloroacetyl-L-2,3-diaminopropanoic acid
-
pH 6.5, 25C
0.019
-
N3-fumaramoyl-L-2,3-diaminopropanoic acid
-
pH 7.5, 37C
0.008
-
N3-Fumaroyl-L-2,3-diaminopropanoic acid
-
pH 7.5, 37C
0.0551
-
N3-Fumaroyl-L-2,3-diaminopropanoic acid
-
pH 7.5, 37C
0.125
-
N3-Fumaroylcarboxyamido-L-2,3-diaminopropionic acid
-
pH 7.5, 37C
-
0.000125
-
N3-iodoacetyl-L-2,3-diaminopropanoic acid
-
pH 6.5, 25C
0.0013
-
UDP-N-acetylglucosamine
-
pH 6.5, 30C
0.0183
-
UDP-N-acetylglucosamine
-
-
0.04
-
UDP-N-acetylglucosamine
-
pH 7.4, 37C
additional information
-
Anticapsin
-
KI varying from 0.001 - 1
IC50 VALUE [mM]
IC50 VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.66
-
(2S)-2-amino-3-(([(2R,3R)-3-benzoyloxiran-2-yl]carbonyl)amino)propanoic acid
-
pH 7.0, 37C
-
0.27
-
(2S)-2-amino-3-([(2E)-4-oxo-4-phenylbut-2-enoyl]amino)propanoic acid
-
pH 7.0, 37C
-
5.6
-
(2S)-2-amino-3-([(2E)-4-oxopent-2-enoyl]amino)propanoic acid
-
pH 7.0, 37C
-
7.3
-
(2S)-3-(([(2R,3R)-3-acetyloxiran-2-yl]carbonyl)amino)-2-aminopropanoic acid
-
pH 7.0, 37C
-
0.056
-
2-amino-2-deoxy-D-glucitol-6-phosphate
-
IC50: 0.056 mM
0.085
-
2-amino-2-deoxy-D-glucitol-6-phosphate
Q6DLZ8
recombinant enzyme, in 10 mM KCl, 1 mg/ml bovine serum albumin, 20 mM imidazole buffer (pH 6.8), 1 mM EDTA, 1 mM dithiothreitol, and 10% (v/v) glycerol
0.12
-
Aaptamine
-
IC50: 0.12 mM
0.1
-
amitrole
-
IC50: 0.1 mM
0.12
-
N3-(4-Methoxyfumaroyl)-L-2,3-diaminopropanoic acid
Q6DLZ8
recombinant enzyme, in 10 mM KCl, 1 mg/ml bovine serum albumin, 20 mM imidazole buffer (pH 6.8), 1 mM EDTA, 1 mM dithiothreitol, and 10% (v/v) glycerol
0.52
-
UDP-N-acetyl-alpha-D-glucosamine
-
pH 7.0, 37C
1.55
-
uridine 5'-diphospho-N-acetyl-D-glucosamine
-
wild-type, pH 6.8, 37C
-
1.7
-
uridine 5'-diphospho-N-acetyl-D-glucosamine
-
mutant Gfa1-His6DELTA343-348, pH 6.8, 37C
-
1.85
-
uridine 5'-diphospho-N-acetyl-D-glucosamine
-
mutant Gfa1-His6DELTA655-660, pH 6.8, 37C
-
2
-
uridine 5'-diphospho-N-acetyl-D-glucosamine
-
mutant Gfa1-K568H/S569H, pH 6.8, 37C
-
0.16
-
uridine 5'-diphospho-N-acetylglucosamine
Q6DLZ8
recombinant enzyme, in 10 mM KCl, 1 mg/ml bovine serum albumin, 20 mM imidazole buffer (pH 6.8), 1 mM EDTA, 1 mM dithiothreitol, and 10% (v/v) glycerol
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.001
-
-
mutant enzyme L468P
0.0047
-
-
-
0.021
-
-
glutamine 6-phosphate-synthetic activity, mutant V711F, pH 7.5, 25C
0.05
-
-
glutamine 6-phosphate-synthetic activity, mutant W97G, pH 7.5, 25C
0.095
-
-
amidohydrolysing activity of the mutant enzyme W97G using D-fructose 6-phosphate as substrate
0.256
-
-
amidohydrolysing activity of the mutant enzyme W97F using D-fructose 6-phosphate as substrate
0.38
-
-
mutant enzyme I271T; mutant enzyme I3T; mutant enzyme S449P
0.39
-
-
wild type enzyme
0.42
-
-
mutant enzyme A38T; mutant enzyme G471S
0.631
-
-
wild type enzyme, using D-fructose 6-phosphate as a substrate
0.89
-
-
amidohydrolysing activity of the wild type enzyme using D-fructose 6-phosphate as substrate
0.94
-
-
amidohydrolysing activity of the mutant enzyme V711F using D-fructose 6-phosphate as substrate
1.2
-
-
glutamine 6-phosphate-synthetic activity, mutant W97F, pH 7.5, 25C
4.66
-
-
-
12
-
-
glutamine 6-phosphate-synthetic activity, wild-type, pH 7.5, 25C
34.8
-
-
-
additional information
-
-
development of an assay for glucosamine 6-phosphate synthase that measures the production of glucosamine 6-phosphate by either following the consumption of acetyl-CoA spectrophotometrically at 230 nm or quantifying the free thiol with 5,5'-dithio-bis(2-nitrobenzoic acid), i.e. Ellmans reagent in a discontinuous manner. Simple assay method, which can be adapted to 96-well microtiter plate format
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6.1
6.4
-
-
6.2
6.7
-
potassium phosphate buffer
6.4
-
Q6DLZ8
-
6.5
7.5
-
-
7
-
-
potassium phosphate buffer
7.2
-
-
TES buffer
7.2
-
-
assay at
7.4
-
-
-
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5.5
7.5
Q6DLZ8
-
6
8
-, Q8G545
marked decrease in activity at pH values below 6.0 and above 8.0
6
8.5
-
-
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
37
-
-
assay at
37
-
-
assay at
37
-
-
assay at
37
-
-
assay at
55
-
-, Q8G545
-
PDB
SCOP
CATH
ORGANISM
Candida albicans (strain SC5314 / ATCC MYA-2876)
Candida albicans (strain SC5314 / ATCC MYA-2876)
Candida albicans (strain SC5314 / ATCC MYA-2876)
Candida albicans (strain SC5314 / ATCC MYA-2876)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Francisella tularensis subsp. tularensis (strain SCHU S4 / Schu 4)
Shewanella denitrificans (strain OS217 / ATCC BAA-1090 / DSM 15013)
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
41000
-
-
glutamine amide-hydrolysing domain, SDS-PAGE
42000
-
-
isomerase domain consisting of residues 346-712, X-ray crystallography
66640
-
-
SDS-PAGE
78400
-
-
SDS-PAGE
79000
-
-
SDS-PAGE, wild-type and mutants
79140
-
-
Superdex 200 HR 10/30 gel filtration
159000
-
-
hexose phosphate-isomerizing domain, Superdex 200 HR 10/30 gel filtration
160000
-
-
gel filtration, mutant Gfa1-His6DELTA655-660
170000
193000
-
gel filtration
280000
-
-
gel filtration
300000
-
-
ultrafiltration
306000
-
Q6DLZ8
estimated from amino acid sequence
310000
-
Q6DLZ8
gel filtration
320000
-
-
gel filtration
328000
-
-
gel filtration, mutant Gfa1-K568H/S569H
335000
-
-
gel filtration, mutant Gfa1-His6DELTA343-348
340000
-
-
gel filtration, preincubated enzyme
340000
-
-
gel filtration, wildtype
350000
-
-
gel filtration
350000
-
-
-
410000
-
-
gel filtration, untreated enzyme
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
? * 77000, SDS-PAGE
?
-, Q8G545
x * 68600, calculated for native protein, x * 69600, calculated, and x * 69400, SDS-PAGE, His-tagged protein, respectively
dimer
-
2 * 70800, SDS-PAGE
dimer
-
2 * 70000, calculated by means of crystalline structure determined by X ray diffraction
dimer
-
sedimentation velocity experiments show that at low concentration the enzyme is mainly present as a dimer. At a higher protein concentration the equilibrium between the two forms of GlmS is significantly displaced toward the oligomeric form
dimer
-
the enzyme is regulated by a morpheein-type allosteric mechanism, in which functional dimeric GlmS is in equilibrium with the inactive hexamer
hexamer
-
the enzyme is regulated by a morpheein-type allosteric mechanism, in which functional dimeric GlmS is in equilibrium with the inactive hexamer
homotetramer
-
4 * 39500, hexose phosphate-isomerizing domain, Superdex 200 HR 10/30 gel filtration
homotetramer
-
4 * 80000, SDS-PAGE
homotetramer
Q6DLZ8
4 * 77000, SDS-PAGE
homotetramer
-
4 * 80000
homotetramer
Volvariella volvacea V1-1
-
4 * 77000, SDS-PAGE
-
oligomer
-
sedimentation velocity experiments show that at low concentration the enzyme is mainly present as a dimer. At a higher protein concentration the equilibrium between the two forms of GlmS is significantly displaced toward the oligomeric form
tetramer
-
4 * 75000, gel filtration, SDS-PAGE
tetramer
P53704
crystallization data
monomer
-
1 * 42000, glutamine amide-hydrolysing domain, Superdex 200 HR 10/30 gel filtration
additional information
-
The fact that the 77 kDa protein expressed in Escherichia coli is sensitive to inhibition by UDP-N-acetylglucosamine is consistent with the idea that mammalian GFAT is comprised of four identical subunits
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
phosphoprotein
-
enzyme is phosphorylated in vivo, phosphorylation site is residue S243. Phosphorylation at Ser243 stimulates glucosamine 6-phosphate synthesizing activity, lowers amidohydrolyzing activity in the absence of fructose 6-phosphate, and lowers Km of fructose 6-phosphate 2fold, but has no effect on UDP-GlcNAc inhibition. Phosphorylation is mediated by AMP-activated protein kinase and calcium/calmodulin-dependent kinase II in vitro
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
crystals are composed of a trans-acting form of the Thermoanaerobacter tengcongensis ribozyme with a single 2'-deoxyribose substitution at the cleavage site, which traps the RNA in the precleavage state. These crystals yield an accurate structure of the RNA to 1.7 A resolution
-
crystal structure of the isomerase domain in complex with the allosteric inhibitor UDP-GlcNAc and in the presence of glucose 6-phosphate, fructose 6-phosphate and an analogue of the reaction intermediate, 2-amino-2-deoxy-D-mannitol 6-phosphate. Deduction of a solution structure of the native protein. The tetrameric enzyme can be described as a dimer of dimers, with each half similar to the related enzyme from Escherichia coli. The core of the protein consists of the isomerase domains
P53704
hanging drop vapour diffusion and sitting drop vapour diffusion in 20% (w/v) PEG 600 and 0.15 M KSCN at pH 8.5
-
crystal structure of intact protein
-
crystal structures of enzyme alone and in complex with the glucosamine 6-phosphate product at 2.95 A and 2.9 A resolution, respectively. No electron density for the glutaminase domain is observed. Upon sugar binding, the C-terminal loop, which forms the major part of the channel walls, becomes ordered and covers the synthase site. The ordering of the glutaminase domains likely follows fructose 6-phosphate binding by the anchoring of Trp74, which acts as the gate of the channel, on the closed C-terminal loop. This is accompanied by a major conformational change of the side chain of Lys503 of the neighboring synthase domain that strengthens the interactions of the synthase domain with the C-terminal loop and completely shields the synthase site. The concomitant conformational change of theLys503-Gly505 tripeptide places catalytic His504 in the proper position to open the sugar and buries the linear sugar, which is now in the vicinity of the catalytic groups involved in the sugar isomerization reaction
-
hanging drop vapour diffusion method, 12% polyethylene glycol 8000, 0.1 M KCl, 5% glycerol
P17169
molecular dynamics simulations. Key role for Trp74, in the sealing of the hydrophobic channel connecting the two binding sites, as well as for the two Ala602 and Val605 residues, which form a narrow passage whose opening/closing constitutes an essential event in ammonia transfer
-
the crystal structure of the C1A mutant of Escherichia coli GlmS, solved at 2.5 A resolution, is organized as a hexamer, where the glutaminase domains adopt an inactive conformation
-
two crystal complexes of the isomerase domain with D-glucose 6-phosphate and 2-amino-2-deoxyglucitol 6-phosphate
-
isomerase domain of the human GFAT in the presence of cyclic glucose-6-phosphate and linear D-glucosamine 6-phosphate, hanging drop vapor diffusion method, at 20C using 12% (v/v) isopropanol, 0.8 M ammonium acetate and 40 mM Tris-HCl at pH 8.5
Q06210
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
37
-
-
90 min, complete loss of activity without stabilizing agent. Dithiothreitol, D-fructose 6-phosphate, D-glucose 6-phosphate or L-glutamine, 1 mM, increase thermal stability at 37C
45
-
Q6DLZ8
half-life of 1 h at 45C
50
-
-
activity of the wild type enzyme is not affected by incubation at 50C for 60 min
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
sucrose needed as stabilizing agent
-
glucose 6-phosphate, 12 mM, required as protective agent during purification
-
inactivated by freezing and thawing
-
inactivated when exposed to a solution of pH 5.5 or below
-
isopropanol, 1%, stabilizes during purification
-
inactivated when exposed to a solution of pH 5.5 or below
-
can be concentrated by precipitation with 2.3 M ammonium sulfate with some concomitant loss of activity
-
extremely unstable during purification
-
inactivated when exposed to a solution of pH 5.5 or below
-
very unstable
-
complete loss of activity after treatment with ammonium sulfate, 30-50% saturation
-
dithiothreitol, D-fructose 6-phosphate, D-glucose 6-phosphate or L-glutamine, 1 mM, increases thermal stability at 37C
-
freezing and thawing has no effect on activity
-
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-20C, 0.6 M sucrose, 60% loss of activity after 45 days
-
0-2C, potassium phosphate buffer, pH 7.0, 0.06 M L-glutamine, 0.01 M EDTA, stable for up to 3 or 4 weeks
-
5C, potassium phosphate buffer, pH 7.5, 1 mM EDTA, 1 mM dithiothreitol, 0.5 mM L-glutamine, 0.05 mM D-glucose 6-phosphate, 600 mM sucrose, stable for few weeks
-
-25C, 1 month, 15% activity loss, ammonium sulfate precipitated enzyme
-
-80C, 50 mM Tris-HCl, pH 7.8, 200 mM NaCl, 1 mM fructose 6-phosphate, 2 mM tris(2-carboxyethyl)phosphine hydrochloride, 200 mM imidazole, 10% glycerol, stable for up to 12 months
-
-18C, little loss of activity after 1 week for lyophilized material after calcium phosphate gel treatment
-
-80C, 3 months
-
4C or -15C, 8 days, 50% activity loss
-
4C or 15C, 50% loss of activity after 8 days
-
4C, 25 mM potassium phosphate buffer, pH 7.5, 1 mM EGTA, 2 mM dithiothreitol, 500 mM sucrose, stable for up to 2 or 3 weeks
-
in liquid N2, stable for up to 2 weeks
-
4C, 50 mM MOPS (pH 6.5), 1 mM dithiothreitol, 1 mM EDTA, and 10 mM KCl, overnight storage, recombinant enzyme activity is low and no longer evident with preparations losing 60% of their activity
Q6DLZ8
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
recombinant protein
-, Q8G545
Ni2+-IDA agarose affinity chromatography and HiTrap desalting column chromatography
-
Ni2+-IDA agarose chromatography
-
Ni2+-IDA agarose chromatography and Superdex 200 gel filtration
-
using one-step immobilized metal-ion affinity chromatography
-
Q-Sepharose fast flow column chromatography and Superdex 200 Hiload gel filtration
P17169
Q-Sepharose fast flow column chromatography and Superdex 200 HR 26/60 Hiload gel filtration
-
Ni-NTA column chromatography
Q06210
Bio-Spin 6 column chromatography
-
enzyme is purified to at least 98% homogeneity with 42% final yield
-
partial purification by immobilized Ni2+ affinity column chromatography
Q6DLZ8
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
expression as His-tagged protein
-, Q8G545
expressed in Escherichia coli BL21(DE3) pLysS cells
-
expressed in Escherichia coli BL21(DE3)pLysS cells
-
expressed in Escherichia coli strain BL21(DE3) pLysS
-
expressed in Saccharomyces cerevisiae strain YRS C-65
-
overexpressed in Escherichia coli
-
expressed in Escherichia coli
-
expressed in Escherichia coli BL21(DE3) cells
Q06210
expression in insect cell and Escherichia coli
-
expressed in Escherichia coli JM109 cells
Q6DLZ8
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
V711F
-
mutation results in an almost complete elimination of the GlcN-6-P-synthetic activity, with the retention of the amidohydrolase and sugar phosphate-isomerizing activities; reduction of the glucosamine 6-phosphate-synthetic activity, with the retention of the amidohydrolase and sugar phosphate-isomerizing activities
W97F
-
mutation results in an almost complete elimination of the GlcN-6-P synthetic activity, with the retention of the amidohydrolase and sugar phosphate-isomerizing activities; reduction of the glucosamine 6-phosphate-synthetic activity, with the retention of the amidohydrolase and sugar phosphate-isomerizing activities. Residue W97 functions as a molecular gate, opening and closing the intramolecular channel that connects the glutamine amide-hydrolysing and hexose phosphate-isomerizing domains
W97G
-
almost complete elimination of the glucosamine 6-phosphate-synthetic activity, with the retention of the amidohydrolase and sugar phosphate-isomerizing activities. Residue W97 functions as a molecular gate, opening and closing the intramolecular channel that connects the glutamine amide-hydrolysing and hexose phosphate-isomerizing domains; mutation results in an almost complete elimination of the GlcN-6-P-synthetic activity, with the retention of the amidohydrolase and sugar phosphate-isomerizing activities
A38T
-
mutant shows increased resistance against glucosamine-6-phosphate
A602L
-
enhanced activity compared to the wild type enzyme, the behaviour of the mutant is similar to that of the wild type counterpart during purification demonstrating no significant modification in the overall protein structure
C1A
-
C1A-GlmS does not reveal glutaminase activity at 37C when tested in the presence of Gln only
C1A
-
the structure of the inactive C1A mutant, crystallized in the presence of D-fructose 6-phosphate and Gln is deterimined. The C1A-GlmS structure is organized as a hexamer. The enzyme is regulated by a morpheein-type allosteric mechanism, in which functional dimeric GlmS is in equilibrium with the inactive hexamer
G471S
-
mutant shows increased resistance against glucosamine-6-phosphate
I271T
-
mutant shows increased resistance against glucosamine-6-phosphate
I3T
-
mutant shows increased resistance against glucosamine-6-phosphate
L468P
-
mutant shows increased resistance against glucosamine-6-phosphate
S449P
-
mutant shows increased resistance against glucosamine-6-phosphate
V605L
-
enhanced activity compared to the wild type enzyme, the behaviour of the mutant is similar to that of the wild type counterpart during purification demonstrating no significant modification in the overall protein structure
W74A
-
efficiency of ammonia transfer is close to zero. No use of ammonia as a substrate; enhanced activity compared to the wild type enzyme, the behaviour of the mutant is similar to that of the wild type counterpart during purification demonstrating no significant modification in the overall protein structure
W74F
-
enhanced activity compared to the wild type enzyme, the behaviour of the mutant is similar to that of the wild type counterpart during purification demonstrating no significant modification in the overall protein structure
W74L
-
decrease in ammonia transfer, 5-7fold increase in the affinity for glutamine in the presence of fructose 6-phosphate; enhanced activity compared to the wild type enzyme, the behaviour of the mutant is similar to that of the wild type counterpart during purification demonstrating no significant modification in the overall protein structure
S243E
-
increase in activity, 2fold lower Km value for D-fructose 6-phosphate than wild-type
G40A
-
mutant with exchanged guanine is inactive. The 2.7 A resolution crystal structure of the mutant shows that the RNA is in a conformation nearly identical to that of the wild-type glmS ribozyme. The experimental electron density maps indicate that GlcN6P binds to the G40A mutant in the same location as in the wild-type ribozyme. Raman pH titrations of GlcN6P using crystals of the G40A mutant glmS ribozyme show that the pKa of the amine of the ribozyme-bound GlcN6P differs substantially for the wild-type and G40A mutant ribozymes
additional information
-
expression of truncated enzyme variants as His-tagged proteins. Fragments encompassing residues 1-345 and 346-712 represent the functional glutamine amide-hydrolysing GAH and hexose phosphate-isomerizing domains ISOM, respectively. The native GAH domain is monomeric, whereas the native ISOM domain forms tetramers, as does the whole enzyme. The binding site for the feedback inhibitor, uridine 5'-diphospho-N-acetyl-D-glucosamine, is located in the ISOM domain. Inhibitor binding affects amidohydrolysing activity of the GAH domain and, as a consequence, the D-glucosamine-6-phosphate-synthetic activity of the whole enzyme. The fragment containing residues 218-283 is neither involved in ligand binding nor in protein oligomerization. An intramolecular channel connects the GAH and ISOM domains. The channel becomes leaky upon deletion of amino acids 709-712 and in the W97F and W97G mutants
additional information
-
three recombinant versions containing internal oligoHis fragments are constructed: (a) by substituting residues 343-348 of the interdomain undecapeptide linker with hexaHis, (b) by replacing solvent-exposed residues 655-660 of the isomerase domain with hexaHis, and (c) by replacing amino acids at positions 568 and 569 with His residues to generate the three-dimensional hexaHis microdomain in the enzyme quaternary structure. The resulting constructs are purified to homogeneity. Catalytic properties are comparable with that of the wild-type enzyme. The construct containing the 655-660 hexaHis insert is found to be a homodimeric protein
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
analysis
-
development of an assay for glucosamine 6-phosphate synthase that measures the production of glucosamine 6-phosphate by either following the consumption of acetyl-CoA spectrophotometrically at 230 nm or quantifying the free thiol with 5,5'-dithio-bis(2-nitrobenzoic acid), i.e. Ellmans reagent in a discontinuous manner. Simple assay method, which can be adapted to 96-well microtiter plate format
medicine
-
target for antifungal agents
medicine
-
mean glutamine:fructose 6-phosphate amidotransferase activity is significantly higher in diabetic compared to control subjects. Plasma levels of diabetic patients also exhibit increased lipid peroxidation and protein carbonylation. Glutamine:fructose 6-phosphate amidotransferase activity is positively correlated with glutamine:fructose 6-phosphate amidotransferase mRNA, HbA1c, insulin resistance, postprandial plasma glucose and levels of thiobarbituric acid reactive substances and protein carbonyl content
medicine
-
hypoxia induces gene expression in phagocyte