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Information on EC 3.5.99.6 - glucosamine-6-phosphate deaminase
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EC Tree
3.5.99.6 glucosamine-6-phosphate deaminaseIUBMB Comments
The enzyme uses ring opening and isomerization of the aldose-ketose type to convert the -CH(-NH2)-CH=O group of glucosamine 6-phosphate into -C(=NH)-CH2-OH, forming 2-deoxy-2-imino-D-arabino-hexitol, which then hydrolyses to yield fructose 6-phosphate and ammonia. N-Acetyl-D-glucosamine 6-phosphate, which is not broken down, activates the enzyme.
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Word Map
- 3.5.99.6
- obesity
- n-acetylglucosamine
-
tmem18
-
kctd15
-
sec16b
-
tfap2b
-
homotropic
-
5.3.1.10
- n-acetylglucosamine-6-phosphate
- d-glucosamine
-
bmi-associated
- naga
- glcnac6p
-
glcnac-6-phosphate
-
lyplal1
-
tnni3k
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
gnpda2, glucosamine-6-phosphate deaminase, oscillin, gnpda1, gnpda, glucosamine-6-phosphate isomerase, glucosamine 6-phosphate deaminase, glcn6p deaminase, glucosamine 6-phosphate isomerase, glucosamine-6-phosphate deaminase 2, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
2-amino-2-deoxy-D-glucose-6-phosphate aminohydrolase (ketol-isomerizing)
-
-
2-amino-2-deoxy-D-glucose-6-phosphate ketol isomerase (deaminating)
-
-
-
-
aminodeoxyglucosephosphate isomerase
-
-
-
-
EC 5.3.1.10
GlcN-6-P isomerase
-
-
-
-
GlcN6P deaminase
glucosamine 6-phosphate deaminase
-
-
-
-
glucosamine 6-phosphate isomerase
-
-
-
-
glucosamine phosphate deaminase
-
-
-
-
glucosamine-6-phosphate deaminase
glucosamine-6-phosphate deaminase 1
glucosamine-6-phosphate isomerase
glucosamine-6P deaminase
glucosamine-P isomerase
-
-
-
-
glucosaminephosphate isomerase
-
-
-
-
GNPDA
GNPDA2
isomerase, glucosamine phosphate
-
-
-
-
NAG1
NagB
NagBBs
oscillin
-
-
-
-
phoshoglucosamine isomerase
-
-
-
-
phosphoglucosaminisomerase
-
-
-
-
SMU.636 protein
EC 5.3.1.10
-
-
formerly
-
GlcN6P deaminase
-
-
-
-
glucosamine-6-phosphate deaminase
-
-
-
-
GNPDA
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
alpha-D-glucosamine 6-phosphate + H2O = D-fructose 6-phosphate + NH3
reaction mechanism involves a ring-opening step, followed by an enolization step that proceeds through a cis-enolamine and its tautomeric imine as reaction intermediates
-
alpha-D-glucosamine 6-phosphate + H2O = D-fructose 6-phosphate + NH3
the mechanism comprises steps to open the pyranose ring of the substrate and a sequence of general base-catalyzed reactions to bring about isomerization and deamination, with Asp72 playing a key role as a proton exchanger
-
alpha-D-glucosamine 6-phosphate + H2O = D-fructose 6-phosphate + NH3
His143 has many functional roles in the active site of enzyme
alpha-D-glucosamine 6-phosphate + H2O = D-fructose 6-phosphate + NH3
thermodynamic study, the allosteric behavior of enzyme can be described by the Monod-Wyman-Changeux model
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alpha-D-glucosamine 6-phosphate + H2O = D-fructose 6-phosphate + NH3
formerly EC 5.3.1.10. Isomerization of the aldose-ketose type converts the -CH(-NH2)-CH=O group of D-glucosamine 6-phosphate into -C(=NH)-CH2-OH, forming 2-deoxy-2-imino-D-arabino-hexitol, which then hydrolyses to yield fructose 6-phosphate and ammonia. N-acetyl-D-glucosamine 6-phosphate, which is not broken down, activates the enzyme
-
-
-
alpha-D-glucosamine 6-phosphate + H2O = D-fructose 6-phosphate + NH3
enzyme-activator and enzyme-inhibitor complex have strucutral differences that also differ from ternary complex enzyme-activator-inhibitor. The occupation of the active site generates structural perturbations which extend to the other subunits, resulting in predominance of the R over the T forms in the population of deaminase hexamers
alpha-D-glucosamine 6-phosphate + H2O = D-fructose 6-phosphate + NH3
residue R172 has a specific role in binding the substrate to the enzyme in the T state
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
group transfer
-
-
transmolecular
-
intramolecular oxidoreduction
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
2-amino-2-deoxy-D-glucose-6-phosphate aminohydrolase (ketol isomerizing)
The enzyme uses ring opening and isomerization of the aldose-ketose type to convert the -CH(-NH2)-CH=O group of glucosamine 6-phosphate into -C(=NH)-CH2-OH, forming 2-deoxy-2-imino-D-arabino-hexitol, which then hydrolyses to yield fructose 6-phosphate and ammonia. N-Acetyl-D-glucosamine 6-phosphate, which is not broken down, activates the enzyme.
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CAS REGISTRY NUMBER
COMMENTARY
9013-10-9
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
D-fructose 6-phosphate + NH3
alpha-D-glucosamine 6-phosphate + H2O
-
-
-
-
r
D-fructose 6-phosphate + NH3
D-glucosamine 6-phosphate + H2O
-
deamination reaction is preferred over amination/isomerization
-
-
r
alpha-D-glucosamine 6-phosphate + H2O
D-fructose 6-phosphate + NH3
-
-
-
?
alpha-D-glucosamine 6-phosphate + H2O
D-fructose 6-phosphate + NH3
-
-
-
?
alpha-D-glucosamine 6-phosphate + H2O
D-fructose 6-phosphate + NH3
-
-
-
?
alpha-D-glucosamine 6-phosphate + H2O
D-fructose 6-phosphate + NH3
-
-
-
-
?
alpha-D-glucosamine 6-phosphate + H2O
D-fructose 6-phosphate + NH3
-
-
-
?
alpha-D-glucosamine 6-phosphate + H2O
D-fructose 6-phosphate + NH3
-
-
-
r
alpha-D-glucosamine 6-phosphate + H2O
D-fructose 6-phosphate + NH3
-
-
-
-
r
alpha-D-glucosamine 6-phosphate + H2O
D-fructose 6-phosphate + NH3
-
-
-
r
alpha-D-glucosamine 6-phosphate + H2O
D-fructose 6-phosphate + NH3
in standard culture conditions keratinocyte GNPDAs mainly catalyze the reaction from GlcN6P back to Fru6P
-
-
r
alpha-D-glucosamine 6-phosphate + H2O
D-fructose 6-phosphate + NH3
-
-
-
?
alpha-D-glucosamine 6-phosphate + H2O
D-fructose 6-phosphate + NH3
Staphylococcus aureus TCH1516
-
-
-
?
alpha-D-glucosamine 6-phosphate + H2O
D-fructose 6-phosphate + NH3
-
-
-
?
D-glucosamine 6-phosphate + H2O
D-fructose 6-phosphate + NH3
-
-
-
?
D-glucosamine 6-phosphate + H2O
D-fructose 6-phosphate + NH3
-
-
-
-
?
D-glucosamine 6-phosphate + H2O
D-fructose 6-phosphate + NH3
-
-
-
-
r
D-glucosamine 6-phosphate + H2O
D-fructose 6-phosphate + NH3
-
-
-
r
D-glucosamine 6-phosphate + H2O
D-fructose 6-phosphate + NH3
-
-
?
D-glucosamine 6-phosphate + H2O
D-fructose 6-phosphate + NH3
-
-
?
D-glucosamine 6-phosphate + H2O
D-fructose 6-phosphate + NH3
-
-
-
?
D-glucosamine 6-phosphate + H2O
D-fructose 6-phosphate + NH3
-
-
r
D-glucosamine 6-phosphate + H2O
D-fructose 6-phosphate + NH3
-
specific for
-
r
D-glucosamine 6-phosphate + H2O
D-fructose 6-phosphate + NH3
-
active towards alpha-anomer, inactive towards the beta-anomer. Strong affinity for the open-chain form of glucosamine 6-phosphate
-
?
D-glucosamine 6-phosphate + H2O
D-fructose 6-phosphate + NH3
-
-
-
?
D-glucosamine 6-phosphate + H2O
D-fructose 6-phosphate + NH3
-
-
-
r
D-glucosamine 6-phosphate + H2O
D-fructose 6-phosphate + NH3
-
-
-
?
D-glucosamine 6-phosphate + H2O
D-fructose 6-phosphate + NH3
-
-
r
D-glucosamine 6-phosphate + H2O
D-fructose 6-phosphate + NH3
-
-
-
?
D-glucosamine 6-phosphate + H2O
D-fructose 6-phosphate + NH3
-
no indication of reversibility is noted
-
ir
D-glucosamine 6-phosphate + H2O
D-fructose 6-phosphate + NH3
-
-
-
?
D-glucosamine 6-phosphate + H2O
D-fructose 6-phosphate + NH3
-
-
-
?
D-glucosamine 6-phosphate + H2O
D-fructose 6-phosphate + NH3
-
deamination reaction is preferred over amination/isomerization
-
-
r
glucosamine 6-phosphate + H2O
fructose 6-phosphate + NH3
-
the main enzyme in Aspergillus niger cells responsible for rapid glucosamine accumulation during the early stages of growth in a high-citric-acid-yielding medium, the enzyme must compete with 6-phosphofructo-1-kinase for the common substrate fructose 6-phosphate in Aspergillus niger cells, role of glucosamine in the pathway regulation, overview
-
-
r
glucosamine 6-phosphate + H2O
fructose 6-phosphate + NH3
-
the main enzyme in Aspergillus niger cells responsible for rapid glucosamine accumulation during the early stages of growth in a high-citric-acid-yielding medium, the enzyme must compete with 6-phosphofructo-1-kinase for the common substrate fructose 6-phosphate in Aspergillus niger cells, role of glucosamine in the pathway regulation, overview
-
-
r
glucosamine 6-phosphate + H2O
fructose 6-phosphate + NH3
-
-
-
-
?
additional information
?
-
-
the enzyme catalyses the first commited step in a biosynthetic pathway leading to amino sugar-nucleotide precursor of bacterial peptidoglycan
-
-
?
additional information
?
-
the enzyme has a remarkable role as the only allosteric enzyme in the amino-sugar catabolic route
-
-
?
additional information
?
-
-
the enzyme has a remarkable role as the only allosteric enzyme in the amino-sugar catabolic route
-
-
?
additional information
?
-
protein-protein interactions of HPr-NagB, U-PII-NagB, and NanE-NagB activate NagB by increasing the affinity of the enzyme for its substrate, GlcN-6P, and/or increasing the Vmax. NagB, glucosamine 6-phosphate deaminase. Protein-protein interactome for NagB, NagB interacts with numerous proteins in the Escherichia coli cell, overview
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-
-
additional information
?
-
-
the activity of the enzyme in erythrocytes is low, indicating that hexosamine catabolism is not a major source of energy in the erythrocyte
-
-
?
additional information
?
-
-
enzyme in spermatozoa may play a role during the acrosome reaction
-
-
?
additional information
?
-
kinetic analysis of NagB is performed using a coupled assay with phosphoglucoisomerase, glucose-6-phosphate dehydrogenase, and NADP+
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-
-
additional information
?
-
Staphylococcus aureus TCH1516
kinetic analysis of NagB is performed using a coupled assay with phosphoglucoisomerase, glucose-6-phosphate dehydrogenase, and NADP+
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-
-
additional information
?
-
kinetic analysis of NagB is performed using a coupled assay with phosphoglucoisomerase, glucose-6-phosphate dehydrogenase, and NADP+
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-
-
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
D-fructose 6-phosphate + NH3
alpha-D-glucosamine 6-phosphate + H2O
-
-
-
-
r
alpha-D-glucosamine 6-phosphate + H2O
D-fructose 6-phosphate + NH3
-
-
-
?
alpha-D-glucosamine 6-phosphate + H2O
D-fructose 6-phosphate + NH3
-
-
-
?
alpha-D-glucosamine 6-phosphate + H2O
D-fructose 6-phosphate + NH3
-
-
-
?
alpha-D-glucosamine 6-phosphate + H2O
D-fructose 6-phosphate + NH3
-
-
-
-
?
alpha-D-glucosamine 6-phosphate + H2O
D-fructose 6-phosphate + NH3
-
-
-
?
alpha-D-glucosamine 6-phosphate + H2O
D-fructose 6-phosphate + NH3
-
-
-
r
alpha-D-glucosamine 6-phosphate + H2O
D-fructose 6-phosphate + NH3
-
-
-
-
r
alpha-D-glucosamine 6-phosphate + H2O
D-fructose 6-phosphate + NH3
-
-
-
r
alpha-D-glucosamine 6-phosphate + H2O
D-fructose 6-phosphate + NH3
in standard culture conditions keratinocyte GNPDAs mainly catalyze the reaction from GlcN6P back to Fru6P
-
-
r
alpha-D-glucosamine 6-phosphate + H2O
D-fructose 6-phosphate + NH3
-
-
-
?
alpha-D-glucosamine 6-phosphate + H2O
D-fructose 6-phosphate + NH3
Staphylococcus aureus TCH1516
-
-
-
?
alpha-D-glucosamine 6-phosphate + H2O
D-fructose 6-phosphate + NH3
-
-
-
?
D-glucosamine 6-phosphate + H2O
D-fructose 6-phosphate + NH3
-
-
-
-
?
D-glucosamine 6-phosphate + H2O
D-fructose 6-phosphate + NH3
-
-
-
-
r
D-glucosamine 6-phosphate + H2O
D-fructose 6-phosphate + NH3
-
-
-
?
glucosamine 6-phosphate + H2O
fructose 6-phosphate + NH3
-
the main enzyme in Aspergillus niger cells responsible for rapid glucosamine accumulation during the early stages of growth in a high-citric-acid-yielding medium, the enzyme must compete with 6-phosphofructo-1-kinase for the common substrate fructose 6-phosphate in Aspergillus niger cells, role of glucosamine in the pathway regulation, overview
-
-
r
glucosamine 6-phosphate + H2O
fructose 6-phosphate + NH3
-
the main enzyme in Aspergillus niger cells responsible for rapid glucosamine accumulation during the early stages of growth in a high-citric-acid-yielding medium, the enzyme must compete with 6-phosphofructo-1-kinase for the common substrate fructose 6-phosphate in Aspergillus niger cells, role of glucosamine in the pathway regulation, overview
-
-
r
glucosamine 6-phosphate + H2O
fructose 6-phosphate + NH3
-
-
-
-
?
additional information
?
-
-
the enzyme catalyses the first commited step in a biosynthetic pathway leading to amino sugar-nucleotide precursor of bacterial peptidoglycan
-
-
?
additional information
?
-
the enzyme has a remarkable role as the only allosteric enzyme in the amino-sugar catabolic route
-
-
?
additional information
?
-
-
the enzyme has a remarkable role as the only allosteric enzyme in the amino-sugar catabolic route
-
-
?
additional information
?
-
protein-protein interactions of HPr-NagB, U-PII-NagB, and NanE-NagB activate NagB by increasing the affinity of the enzyme for its substrate, GlcN-6P, and/or increasing the Vmax. NagB, glucosamine 6-phosphate deaminase. Protein-protein interactome for NagB, NagB interacts with numerous proteins in the Escherichia coli cell, overview
-
-
-
additional information
?
-
-
the activity of the enzyme in erythrocytes is low, indicating that hexosamine catabolism is not a major source of energy in the erythrocyte
-
-
?
additional information
?
-
-
enzyme in spermatozoa may play a role during the acrosome reaction
-
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Zn2+
required, the sigmoidal response with respect to Zn2+ concentration suggests cooperativity and the binding of at least two metal ions within the active site
additional information
additional information
-
the enzyme is not affected by ammonium ions at 5-20 mM
additional information
-
Mn2+, Hg2+, Mg2+, Co2+ and Ni2+ enhance in decreasing order the activity in both directions
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
diethyl dicarbonate
complete inactivation, 2-deoxy-2-amino-D-glucitol 6-phosphate protects
UDP-N-acetylglucosamine
-
slight inhibition at 1.67 mM, slight activation at 0.00167-0.167 mM
PCMB
-
protection by 0.3 mM glucosamine 6-phosphate, no protection by 0.3 mM N-acetylglucosamine 6-phosphate
additional information
not: alpha and beta O-methyl glycoside of D-fructose 6-phosphate
-
additional information
-
not: alpha and beta O-methyl glycoside of D-fructose 6-phosphate
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
UDP-N-acetylglucosamine
-
slight activation at 0.00167-0.167 mM, slight inhibition at 1.67 mM
N-acetylglucosamine 6-phosphate
-
activator of the enzyme in amination direction, leads to about 30% increased activity at 0.07-0.14 mM, overview
N-acetylglucosamine 6-phosphate
-
activates enzyme by increasing its kcat without any change in the Km values for D-glucosamine 6-phosphate
N-acetylglucosamine 6-phosphate
-
the cooperativity of the reaction is completely abolished by saturating concentrations of GlcNAcGP, this allosteric modulator activated the reaction with a typical K-effect, overview
N-acetylglucosamine 6-phosphate
-
increases reaction velocity when D-glucosamine 6-phosphate is present at levels below that required for saturation
N-acetylglucosamine 6-phosphate
GlcNAc6P, allosteric site ligand, behaving as a V activator and a K inhibitor: in the absence of GlcNAc6P, the apparent kcat of the enzyme is so low, that GlcNAc6P behaves as an essential activator. Additionally, substrate inhibition, dependent on GlcNAc6P concentration, is observed, Monod allosteric model with some additional postulates, overview. The ligand binds to either enzyme conformational state, but with higher affinity for the R form
additional information
-
enzyme contains 5 half-cystines per monomer, the sulfhydryls are not essential for catalysis or allosteric behavior of the enzyme
-
additional information
-
each subunit has for Cys residues located at positions 118, 219, 228 and 239, Cys118 and Cys239 form a pair of vicinal thiols
-
additional information
NanE, GlcNAc-6P epimerase, and the uridylylated PII protein allosterically activate NagB by direct protein-protein interactions, overview. Uridylylated PII (but not underivatized PII) activates NagB about 10fold at low concentrations of substrate, whereas NanE increases NagB activity about 2fold. NanE activates NagB in the absence or presence of GlcNAc-6P, but histidine-phosphorylatable phosphocarrier protein (HPr) and U-PII activation requires the presence of GlcNAc-6P. NanE-dependent activation of NagB is not dependent on GlcNAc-6P. Activation of NagB by HPr and uridylylated PII, as well as by NanE and HPr (but not by NanE and U-PII), is synergistic, and the modeling, which suggests specific residues involved in complex formation, provides possible explanations. The uridylylated PII protein (U-PII) is generated by posttranslational modification under nitrogen-limiting conditions involving the glutamine/2-oxoglutarate ratio-sensing uridylyltransferase/uridylyl-removing enzyme GlnD. PII (GlnB)-dependent activation of NagB depends on the uridylylation state of GlnB, kinetics for NagB in the presence of PII at different stages of PII modification involving uridylylation by GlnD, overview. The effect is greater at pH 7.5 than at pH 8 due to the allosteric behavior of the Ser-1 mutant NagB, resulting from an increased Hill coefficient, also noticed for the wild-type NagB. Modeling of HPr/U-PII and of HPr/NanE binding to NagB. The PII protein is known to be a regulator of both the activity and the synthesis of glutamine synthetase (GlnA) in enteric bacteria, and of nitrogen metabolism in many other bacteria, archaea, and eukaryotes, in response to the availability of nitrogen sources
-
additional information
-
enzyme activity is not modified by GlcNAc6P, UDPGlcNAc, or UDP-GalNAc
-
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Asthma
Obese individuals experience wheezing without asthma but not asthma without wheezing: a Mendelian randomisation study of 85?437 adults from the Copenhagen General Population Study.
Candidiasis
Attenuation of virulence and changes in morphology in Candida albicans by disruption of the N-acetylglucosamine catabolic pathway.
Carcinoma, Hepatocellular
Erratum: Glucosamine-6-Phosphate Isomerase 1 Promotes Tumor Progression and Indicates Poor Prognosis in Hepatocellular Carcinoma [Corrigendum].
Carcinoma, Hepatocellular
Glucosamine-6-Phosphate Isomerase 1 Promotes Tumor Progression and Indicates Poor Prognosis in Hepatocellular Carcinoma.
Colorectal Neoplasms
Identification of differential proteins in colorectal cancer cells treated with caffeic acid phenethyl ester.
Colorectal Neoplasms
Susceptibility variants for obesity and colorectal cancer risk: The multiethnic cohort and PAGE studies.