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Information on EC 2.6.1.16 - glutamine-fructose-6-phosphate transaminase (isomerizing) and Organism(s) Pseudomonas aeruginosa

for references in articles please use BRENDA:EC2.6.1.16
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EC Tree
IUBMB Comments
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).
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Select one or more organisms in this record: ?
This record set is specific for:
Pseudomonas aeruginosa
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Word Map
The taxonomic range for the selected organisms is: Pseudomonas aeruginosa
The enzyme appears in selected viruses and cellular organisms
Synonyms
gfpt1, gfat1, glms ribozyme, glucosamine-6-phosphate synthase, glutamine:fructose-6-phosphate amidotransferase, glcn-6-p synthase, gfat2, glutamine fructose-6-phosphate amidotransferase, g-6-p synthase, glucosamine 6-phosphate synthase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2-amino-2-deoxy-D-glucose-6-phosphate ketol-isomerase
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GFAT
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glucosamine 6-phosphate synthase
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glucosamine 6-phosphate synthetase
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glucosamine phosphate isomerase (glutamine-forming)
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glucosamine synthase
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glucosamine-6-phosphate isomerase (glutamine-forming)
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glucosamine-6-phosphate synthase
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glucosamine-6-phosphate synthetase
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glucosamine:fructose-6-phosphate aminotransferase
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glutamine-fructose 6-phosphate amidotransferase
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glutamine-fructose 6-phosphate aminotransferase
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glutamine:fructose-6-phosphate aminotransferase
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hexosephosphate aminotransferase
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isomerase, glucosamine phosphate (glutamine-forming)
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L-glutamine fructose 6-phosphate transamidase
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
amino group transfer
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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).
CAS REGISTRY NUMBER
COMMENTARY hide
9030-45-9
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
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
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
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
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-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(3R,4S)-4-(methylamino)-1-phenylpent-1-en-3-ol
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(4S)-2-methyl-2-phenylpentane-1,4-diol
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1,1'-dithiodiformamidine
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irreversible inhibition
2-(4-hydroxyphenyl)-4-(4-nitrophenylimino)chroman-5,7-diol
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3-(tert-butoxycarbonyl)-6-(3-benzoylprop-2-yl)phenol
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4-(1,3-dihydroxypropan-2-ylimino)-2-(4-hydroxyphenyl)chroman-5,7-diol
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4-(2-chlorophenylimino)-2-(4-hydroxyphenyl)chroman-5,7-diol
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4-(2-fluorophenylimino)-2-(4-hydroxyphenyl)chroman-5,7-diol
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5,5'-dithionitrobenzoic acid
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irreversible inhibition
6,6'-Dithiodinicotinic acid
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irreversible inhibition
7-methoxy-2,3-dihydro-2-phenyl-4 quinolone
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anticapsin
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L-glutamine protects, irreversible inhibition
iodoacetamide
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irreversible inhibition
N-ethylmaleimide
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irreversible inhibition
additional information
synthesis of naringenin derivatives with potent glucosamine-6-phosphate synthase inhibitory capacities and antioxidant, antimicrobial, and preservative efficacy. Molecular docking and in silico ADMET analysis, structure-activity relationship studies, overview. MIC values for growth inhibition of the cells
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.85
L-glutamine
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pH 7.5, 37°C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00011
anticapsin
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pH 7.5, 37°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
in vivo assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
glucosamine-6-phosphate synthase is an important enzyme for bacterial and fungal cell wall synthesis
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
A0A509J935_PSEAI
611
0
66317
TrEMBL
-
A0A069Q6H5_PSEAI
340
0
36095
TrEMBL
-
A0A7M3ASU3_PSEAI
611
0
66313
TrEMBL
-
A0A8G4KEN8_PSEAI
611
0
66343
TrEMBL
-
A0A8G6ZGG0_PSEAI
611
0
66355
TrEMBL
-
A0A431XIF3_PSEAI
611
0
66332
TrEMBL
-
A0A241XPH6_PSEAI
611
0
66355
TrEMBL
-
A0A8G6HJI5_PSEAI
611
0
66274
TrEMBL
-
A0A8G3W2A6_PSEAI
611
0
66355
TrEMBL
-
A0A8F9NQH2_PSEAI
611
0
66272
TrEMBL
-
A0A8G6M1Y8_PSEAI
611
0
66385
TrEMBL
-
A0A8G2TS55_PSEAI
611
0
66343
TrEMBL
-
A0A444M016_PSEAI
611
0
66269
TrEMBL
-
A0A2R4KRB8_PSEAI
340
0
36180
TrEMBL
-
A0A8G5R9U1_PSEAI
611
0
66269
TrEMBL
-
A0A072ZGX2_PSEAI
611
0
66327
TrEMBL
-
A0A2R3IPH5_PSEAI
611
0
66337
TrEMBL
-
A0A5D5A125_PSEAI
611
0
66313
TrEMBL
-
A0A6B1YFG6_PSEAI
611
0
66357
TrEMBL
-
A0A8G5QF90_PSEAI
611
0
66317
TrEMBL
-
A0A6A9JV45_PSEAI
611
0
66252
TrEMBL
-
A0A8B4ZTJ5_PSEAI
611
0
66309
TrEMBL
-
A0A8E5UP06_PSEAI
611
0
66341
TrEMBL
-
A0A8G3YDQ0_PSEAI
611
0
66228
TrEMBL
-
A0A8G7A441_PSEAI
611
0
66357
TrEMBL
-
A0A367MDX0_PSEAI
611
0
66295
TrEMBL
-
A0A485GYQ6_PSEAI
611
0
66341
TrEMBL
-
A0A8G6UHS8_PSEAI
611
0
66297
TrEMBL
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Chmara, H.; Zhner, H.
The inactivation of glucosamine synthetase from bacteria by anticapsin, the C-terminal epoxyamino acid of the antibiotic tetaine
Biochim. Biophys. Acta
787
45-52
1984
Bacillus thuringiensis, Escherichia coli, Paenarthrobacter aurescens, Pseudomonas aeruginosa
Manually annotated by BRENDA team
Lather, A.; Sharma, S.; Khatkar, A.
Naringenin derivatives as glucosamine-6-phosphate synthase inhibitors synthesis, antioxidants, antimicrobial, preservative efficacy, molecular docking and in silico ADMET analysis
BMC Chem.
14
41
2020
Aspergillus niger (A2QH83), Aspergillus niger, Proteus mirabilis (B4F0F0), Proteus mirabilis, Escherichia coli (P17169), Escherichia coli, Candida albicans (P53704), Candida albicans, Staphylococcus aureus (Q6GES3), Staphylococcus aureus, Pseudomonas aeruginosa (Q9HT25), Pseudomonas aeruginosa ATCC 15692 (Q9HT25), Staphylococcus aureus MRSA252 (Q6GES3), Proteus mirabilis HI4320 (B4F0F0), Pseudomonas aeruginosa 1C (Q9HT25), Candida albicans ATCC MYA-2876 (P53704), Pseudomonas aeruginosa PRS 101 (Q9HT25), Aspergillus niger FGSC A1513 (A2QH83), Pseudomonas aeruginosa DSM 22644 (Q9HT25), Pseudomonas aeruginosa CIP 104116 (Q9HT25), Pseudomonas aeruginosa LMG 12228 (Q9HT25), Aspergillus niger CBS 513.88 (A2QH83), Pseudomonas aeruginosa JCM 14847 (Q9HT25)
Manually annotated by BRENDA team