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Information on EC 2.3.1.4 - glucosamine-phosphate N-acetyltransferase and Organism(s) Homo sapiens and UniProt Accession Q96EK6

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Homo sapiens
UNIPROT: Q96EK6 not found.
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Word Map
The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected viruses and cellular organisms
Synonyms
glucosamine-6-phosphate n-acetyltransferase, glucosamine-phosphate n-acetyltransferase, glucosamine 6-phosphate n-acetyltransferase, glucosamine-6-phosphate acetyltransferase, glucosamine-6-phosphate n-acetyltransferase 1, osgna1, hsgna1, glcnac-6-phosphate n-acetyltransferase, glucosamine 6-phosphate acetylase, scgna1, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glucosamine-6-phosphate N-acetyltransferase
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glucosamine-6-phosphate N-acetyltransferase 1
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acetyltransferase, glucosamine phosphate
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aminodeoxyglucosephosphate acetyltransferase
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D-glucosamine-6-P N-acetyltransferase
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glucosamine 6-phosphate acetylase
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glucosamine 6-phosphate N-acetyltransferase
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glucosamine phosphate acetyltransferase
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glucosamine-6-phosphate acetylase
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N-acetylglucosamine-6-phosphate synthase
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-
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phosphoglucosamine acetylase
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phosphoglucosamine N-acetylase
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phosphoglucosamine transacetylase
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Acyl group transfer
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PATHWAY SOURCE
PATHWAYS
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-, -
SYSTEMATIC NAME
IUBMB Comments
acetyl-CoA:D-glucosamine-6-phosphate N-acetyltransferase
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CAS REGISTRY NUMBER
COMMENTARY hide
9031-91-8
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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
acetyl-CoA + D-glucosamine 6-phosphate
CoA + N-acetyl-D-glucosamine 6-phosphate
show the reaction diagram
butanoyl-CoA + D-glucosamine 6-phosphate
CoA + N-butanoyl-D-glucosamine 6-phosphate
show the reaction diagram
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-
-
?
isobutanoyl-CoA + D-glucosamine 6-phosphate
CoA + N-isobutanoyl-D-glucosamine 6-phosphate
show the reaction diagram
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-
-
?
propionyl-CoA + D-glucosamine 6-phosphate
CoA + N-propionyl-D-glucosamine 6-phosphate
show the reaction diagram
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-
-
?
acetyl-CoA + D-glucosamine 6-phosphate
CoA + N-acetyl-D-glucosamine 6-phosphate
show the reaction diagram
additional information
?
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ratio of butanoyl-to-acetyltransferase activity for wild-type: 0.6. No substrates: isovaleryl-CoA and decanoyl-CoA
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
p-hydroxymercuribenzoate
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2.5 mM, 81% inhibition of isoenzyme 1, 92% inhibition of isoenzyme 2 and 92.5% inhibition of isoenzyme 3, inhibition by 1.25 mM is reversible upon addition of 2.5 mM dithiothreitol
additional information
not inhibitory: 1,22-bis(3-methyl-1H-imidazolium-1-yl)docosane dimesylate, N-butanoylglucosaminex02beta-S-2-naphthyl
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.026
acetyl-CoA
wild-type
0.097 - 1.2
D-glucosamine 6-phosphate
0.13
propionyl-CoA
pH 7.6, 37°C
0.157 - 0.28
acetyl-CoA
3 - 7.1
D-glucosamine 6-phosphate
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
9 - 22.1
D-glucosamine 6-phosphate
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.00447
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isoenzymes 1 and 2
0.0379
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isoenzyme 3
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5
assay at
9.7
-
in glycine-NaOH
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
assay at
additional information
assay carried out at room temperature
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SwissProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
lack of GNA1 influences cell adhesion and restoration of its function rescues the biological defect
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
GNA1_HUMAN
184
0
20749
Swiss-Prot
other Location (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25000
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2 * 25000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
HsGNA1 forms a tight dimer shown by crystal structure analysis: Each monomer is composed of 184 residues and the monomer structure belongs to a classic GNAT fold of a/b protein, containing all four motifs (C, D, A and B) conserved among the GNATs. Motif C (b1, g2 and a2) and Motif D (b2 and b3) are located next to and interact with each other, contributing to the hydrophobic core. Motif B (b5 and a5) make up part of the active site. Strands b1-b4 form an antiparallel beta sheet, and helices a1-a4, g1 and g2 are flanked on both sides of the central beta sheet. The HsGNA1 dimer is constructed by joining two subunits such that the C-terminal strand b6 projects to the other subunit. The b6-strand swaps between subunits in a dimer. The loop between strands b3 and b4 also extends to the other subunit, contributing to GlcN6P binding. In each subunit, the AcCoA binding cleft is formed by the diverging strands b4 and b5
homodimer
crystal structure
dimer
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2 * 25000, SDS-PAGE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structures of HsGNA1 in its apo form, complexed with GlcN6P, and the E156A mutant are solved and refined to 2.7 A, 2.3 A and 2.0 A resolution, respectively. Results reveal new features of the GlcN6P binding in HsGNA1. The conserved charge distribution at the GlcN6P binding pocket is important for the acceptor substrate affinity. Glu156, a conserved residue present in GNA1 from various eukaryotic organisms, plays an important role in both the catalytic reaction and substrate affinity. Moreover, the GlcN6P binds to GNA1 without the help of AcCoA binding, suggesting that a pseudo-substrate could bind GNA1 as an inhibitor without the help of AcCoA
crystal structures of human and Aspergillus fumigatus GNA1 are determined: structural differences between the two enzymes are mostly located to the sugar-binding site, whereas the AcCoA-binding site is more conserved. These changes affect not only the electrostatics, but also reveal a more spacious sugar binding site in the Aspergillus fumigatus GNA1 enzyme, whereas large side chains at these positions create a tighter pocket in the HsGNA1 enzyme
hanging-drop vapour-diffusion method. The crystal diffract to better than 2.6 A resolution and belong to space group P4(1)2(1)2 or P4(3)2(1)2. The unit-cell parameters are a = b = 50.08, c = 142.88 A
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C157A
mutant shows activities of both acetyl- and butyryltransfer, in the range of the wild type enzyme activity
E156A
Km: 1.2 mM (substrate: glucosamine 6-phosphate), kcat = 9.7/sec (substrate: glucosamine 6-phosphate)
E156D
Km: 0.175 mM (substrate: glucosamine 6-phosphate), kcat = 19.3/sec (substrate: glucosamine 6-phosphate)
L138A
mutant shows activities of both acetyl- and butyryltransfer, in the range of the wild type enzyme activity. Ratio of butanoyl-to-acetyltransferase activity is increased to 1
L155A
mutant shows activities of both acetyl- and butyryltransfer, in the range of the wild type enzyme activity
L155A/N161A
mutant shows activities of both acetyl- and butyryltransfer, in the range of the wild type enzyme activity
L155G
mutant shows activities of both acetyl- and butyryltransfer, in the range of the wild type enzyme activity. Ratio of butanoyl-to-acetyltransferase activity is increased to 0.9
L155G/N161A
mutant shows activities of both acetyl- and butyryltransfer, in the range of the wild type enzyme activity. Ratio of butanoyl-to-acetyltransferase activity is increased to 0.85
L158A
mutant shows activities of both acetyl- and butyryltransfer, in the range of the wild type enzyme activity
L158A/N161A
mutant shows activities of both acetyl- and butyryltransfer, in the range of the wild type enzyme activity
L158G
mutant shows activities of both acetyl- and butyryltransfer, in the range of the wild type enzyme activity
L158G/N161A
mutant shows activities of both acetyl- and butyryltransfer, in the range of the wild type enzyme activity
N161A
mutant shows activities of both acetyl- and butyryltransfer, in the range of the wild type enzyme activity
P159A
mutant shows activities of both acetyl- and butyryltransfer, in the range of the wild type enzyme activity
Y165A
mutant shows activities of both acetyl- and butyryltransfer, in the range of the wild type enzyme activity. Ratio of butanoyl-to-acetyltransferase activity is increased to 0.9
Y165T
mutant shows activities of both acetyl- and butyryltransfer, in the range of the wild type enzyme activity. Ratio of butanoyl-to-acetyltransferase activity is increased to 0.9
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
using affinity, ion-exchange and size-exclusion chromatography: yield 25 mg of pure HsGNA1 per litre of bacterial culture
isoenzymes 1-3, CM-Sephadex
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli as a His-tagged-fusion protein
expression in Escherichia coli
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
treatment with abraxane results in downregulation of expression
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
development of a fluorescence assay where reactive thiols of CoA, generated from the acyl transfer reaction, are monitored using monobromobimane
medicine
analysis of the global protein expression profiles of lung cancer cell A549 treated with abraxane and paclitaxel. The superior drug effect of abraxane is mainly due to the downregulation of GNA1, which causes proliferative delay and cell adhesion defect
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Davison, E.A.; Blumenthal, H.J.; Roseman, S.
Glucosamine metabolism. II. Studies on glucosamine 6-phosphate N-acetylase
J. Biol. Chem.
226
125-133
1957
Canis lupus familiaris, Homo sapiens, Neurospora crassa, Oryctolagus cuniculus, Penicillium sp., Streptococcus sp.
Manually annotated by BRENDA team
Vessal, M.; Jaberi-Pour, M.
Partial purification and kinetic properties of three different D-glucosamine 6-P:N-acetyltransferase forms from human placenta
Comp. Biochem. Physiol. B
121B
379-384
1998
Homo sapiens
-
Manually annotated by BRENDA team
Wang, J.; Zhou, Y.F.; Li, L.F.; Liang, Y.H.; Su, X.D.
Purification, crystallization and preliminary X-ray analysis of the glucosamine-6-phosphate N-acetyltransferase from human liver
Acta Crystallogr. Sect. F
62
1097-1099
2006
Homo sapiens
Manually annotated by BRENDA team
Hurtado-Guerrero, R.; Raimi, O.G.; Min, J.; Zeng, H.; Vallius, L.; Shepherd, S.; Ibrahim, A.F.; Wu, H.; Plotnikov, A.N.; van Aalten, D.M.
Structural and kinetic differences between human and Aspergillus fumigatus D-glucosamine-6-phosphate N-acetyltransferase
Biochem. J.
415
217-223
2008
Aspergillus fumigatus, Homo sapiens (Q96EK6)
Manually annotated by BRENDA team
Wang, J.; Liu, X.; Liang, Y.H.; Li, L.F.; Su, X.D.
Acceptor substrate binding revealed by crystal structure of human glucosamine-6-phosphate N-acetyltransferase 1
FEBS Lett.
582
2973-2978
2008
Homo sapiens (Q96EK6), Homo sapiens
Manually annotated by BRENDA team
Brockhausen, I.; Nair, D.G.; Chen, M.; Yang, X.; Allingham, J.S.; Szarek, W.A.; Anastassiades, T.
Human acetyl-CoA glucosamine-6-phosphate N-acetyltransferase 1 has a relaxed donor specificity and transfers acyl groups up to four carbons in length
Biochem. Cell Biol.
94
197-204
2016
Homo sapiens (Q96EK6)
Manually annotated by BRENDA team
Zhao, M.; Li, H.; Ma, Y.; Gong, H.; Yang, S.; Fang, Q.; Hu, Z.
Nanoparticle abraxane possesses impaired proliferation in A549 cells due to the underexpression of glucosamine 6-phosphate N-acetyltransferase 1 (GNPNAT1/GNA1)
Int. J. Nanomedicine
12
1685-1697
2017
Homo sapiens (Q96EK6)
-
Manually annotated by BRENDA team