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Information on EC 3.5.99.6 - glucosamine-6-phosphate deaminase and Organism(s) Bacillus subtilis and UniProt Accession O35000
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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
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bmi-associated
- naga
- glcnac6p
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glcnac-6-phosphate
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lyplal1
-
tnni3k
The taxonomic range for the selected organisms is: Bacillus subtilis
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
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-6p deaminase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
2-amino-2-deoxy-D-glucose-6-phosphate ketol isomerase (deaminating)
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-
-
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aminodeoxyglucosephosphate isomerase
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-
-
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GlcN-6-P isomerase
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-
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GlcN6P deaminase
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-
-
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glucosamine 6-phosphate deaminase
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-
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glucosamine 6-phosphate isomerase
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-
-
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glucosamine phosphate deaminase
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-
-
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glucosamine-6-phosphate deaminase
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-
-
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glucosamine-P isomerase
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-
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glucosaminephosphate isomerase
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-
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GNPDA
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-
-
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isomerase, glucosamine phosphate
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-
-
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oscillin
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-
-
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phoshoglucosamine isomerase
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-
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phosphoglucosaminisomerase
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-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
intramolecular oxidoreduction
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-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -, -, -
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.
CAS REGISTRY NUMBER
COMMENTARY
9013-10-9
-
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
alpha-D-glucosamine 6-phosphate + H2O
D-fructose 6-phosphate + NH3
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-
-
?
additional information
?
-
-
the enzyme catalyses the first commited step in a biosynthetic pathway leading to amino sugar-nucleotide precursor of bacterial peptidoglycan
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-
?
D-glucosamine 6-phosphate + H2O
D-fructose 6-phosphate + NH3
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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
alpha-D-glucosamine 6-phosphate + H2O
D-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
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.5
alpha-D-glucosamine 6-phosphate
recombinant enzyme, pH 7.4, 37°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
110
alpha-D-glucosamine 6-phosphate
recombinant enzyme, pH 7.4, 37°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
73.3
alpha-D-glucosamine 6-phosphate
recombinant enzyme, pH 7.4, 37°C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
PDB
SCOP
CATH
UNIPROT
ORGANISM
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
recombinant expression of the nonallosteric Bacillus subtilis homologue NagBBs in the NagBEC deficient Escherichia coli mutant, no effects on growth rates or competitive fitness on glucose or the amino sugars are detected, nor is any effect on the concentrations of central metabolites detected, thus demonstrating the robustness of amino sugar metabolism and leaving open the question of the role of allostery in the regulation of NagB
additional information
-
recombinant expression of the nonallosteric Bacillus subtilis homologue NagBBs in the NagBEC deficient Escherichia coli mutant, no effects on growth rates or competitive fitness on glucose or the amino sugars are detected, nor is any effect on the concentrations of central metabolites detected, thus demonstrating the robustness of amino sugar metabolism and leaving open the question of the role of allostery in the regulation of NagB
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene nagB, recombinant expression of the nonallosteric Bacillus subtilis homologue NagBBs in the NagBEC deficient Escherichia coli mutant, resulting in LAA195 (nagBBs+)
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Chmara, H.; Milewski, S.; Andruszkiewicz, R.; Mignini, F.; Borowski, E.
Antibacterial action of dipeptides containing an inhibitor of glucosamine-6-phosphate isomerase
Microbiology
144
1349-1358
1998
Bacillus subtilis
Vincent, F.; Davies, G.J.; Brannigan, J.A.
Structure and kinetics of a monomeric glucosamine 6-phosphate deaminase: missing link of the NagB superfamily?
J. Biol. Chem.
280
19649-19655
2005
Bacillus subtilis
Alvarez-Anorve, L.I.; Gaugue, I.; Link, H.; Marcos-Viquez, J.; Diaz-Jimenez, D.M.; Zonszein, S.; Bustos-Jaimes, I.; Schmitz-Afonso, I.; Calcagno, M.L.; Plumbridge, J.
Allosteric activation of Escherichia coli glucosamine-6-phosphate deaminase (NagB) in vivo justified by intracellular amino sugar metabolite concentrations
J. Bacteriol.
198
1610-1620
2016
Bacillus subtilis (O35000), Bacillus subtilis, Bacillus subtilis 168 (O35000), Escherichia coli (P0A759), Escherichia coli
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