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acetyl-CoA + D-glucosamine 6-phosphate
CoA + N-acetyl-D-glucosamine 6-phosphate
butanoyl-CoA + D-glucosamine 6-phosphate
CoA + N-butanoyl-D-glucosamine 6-phosphate
-
-
-
?
isobutanoyl-CoA + D-glucosamine 6-phosphate
CoA + N-isobutanoyl-D-glucosamine 6-phosphate
-
-
-
?
propionyl-CoA + D-glucosamine 6-phosphate
CoA + N-propionyl-D-glucosamine 6-phosphate
additional information
?
-
acetyl-CoA + D-glucosamine 6-phosphate
CoA + N-acetyl-D-glucosamine 6-phosphate
-
-
-
-
?
acetyl-CoA + D-glucosamine 6-phosphate
CoA + N-acetyl-D-glucosamine 6-phosphate
-
-
-
?
acetyl-CoA + D-glucosamine 6-phosphate
CoA + N-acetyl-D-glucosamine 6-phosphate
-
-
-
-
?
acetyl-CoA + D-glucosamine 6-phosphate
CoA + N-acetyl-D-glucosamine 6-phosphate
-
-
-
-
?
acetyl-CoA + D-glucosamine 6-phosphate
CoA + N-acetyl-D-glucosamine 6-phosphate
-
-
-
-
?
acetyl-CoA + D-glucosamine 6-phosphate
CoA + N-acetyl-D-glucosamine 6-phosphate
-
-
-
?
acetyl-CoA + D-glucosamine 6-phosphate
CoA + N-acetyl-D-glucosamine 6-phosphate
-
catalyzes a step in the biosynthesis of uridine 5'-diphosphate-N-acetyl D-glucosamine
-
?
acetyl-CoA + D-glucosamine 6-phosphate
CoA + N-acetyl-D-glucosamine 6-phosphate
-
-
-
?
acetyl-CoA + D-glucosamine 6-phosphate
CoA + N-acetyl-D-glucosamine 6-phosphate
-
-
-
?
acetyl-CoA + D-glucosamine 6-phosphate
CoA + N-acetyl-D-glucosamine 6-phosphate
-
-
-
?
acetyl-CoA + D-glucosamine 6-phosphate
CoA + N-acetyl-D-glucosamine 6-phosphate
-
-
-
?
acetyl-CoA + D-glucosamine 6-phosphate
CoA + N-acetyl-D-glucosamine 6-phosphate
-
-
-
-
?
acetyl-CoA + D-glucosamine 6-phosphate
CoA + N-acetyl-D-glucosamine 6-phosphate
-
key enzyme in cyst wall polysaccharide biosynthesis, induced at the transcriptional level
-
-
?
acetyl-CoA + D-glucosamine 6-phosphate
CoA + N-acetyl-D-glucosamine 6-phosphate
-
-
-
?
acetyl-CoA + D-glucosamine 6-phosphate
CoA + N-acetyl-D-glucosamine 6-phosphate
-
-
-
?
acetyl-CoA + D-glucosamine 6-phosphate
CoA + N-acetyl-D-glucosamine 6-phosphate
-
-
-
?
acetyl-CoA + D-glucosamine 6-phosphate
CoA + N-acetyl-D-glucosamine 6-phosphate
-
-
-
-
?
acetyl-CoA + D-glucosamine 6-phosphate
CoA + N-acetyl-D-glucosamine 6-phosphate
-
-
-
?
acetyl-CoA + D-glucosamine 6-phosphate
CoA + N-acetyl-D-glucosamine 6-phosphate
-
-
-
-
?
acetyl-CoA + D-glucosamine 6-phosphate
CoA + N-acetyl-D-glucosamine 6-phosphate
-
-
?
acetyl-CoA + D-glucosamine 6-phosphate
CoA + N-acetyl-D-glucosamine 6-phosphate
-
-
-
-
?
acetyl-CoA + D-glucosamine 6-phosphate
CoA + N-acetyl-D-glucosamine 6-phosphate
-
-
-
-
?
acetyl-CoA + D-glucosamine 6-phosphate
CoA + N-acetyl-D-glucosamine 6-phosphate
-
-
-
?
acetyl-CoA + D-glucosamine 6-phosphate
CoA + N-acetyl-D-glucosamine 6-phosphate
-
-
-
?
acetyl-CoA + D-glucosamine 6-phosphate
CoA + N-acetyl-D-glucosamine 6-phosphate
-
-
-
?
acetyl-CoA + D-glucosamine 6-phosphate
CoA + N-acetyl-D-glucosamine 6-phosphate
-
-
-
?
acetyl-CoA + D-glucosamine 6-phosphate
CoA + N-acetyl-D-glucosamine 6-phosphate
-
-
-
?
acetyl-CoA + D-glucosamine 6-phosphate
CoA + N-acetyl-D-glucosamine 6-phosphate
-
-
-
-
?
acetyl-CoA + D-glucosamine 6-phosphate
CoA + N-acetyl-D-glucosamine 6-phosphate
-
enzyme is involved in de novo UDP-N-acetylglucosamine biosynthesis. Aberrant root morphology of the gna1 mutant includes shortening of roots, disruption of microtubules, and shrinkage of cells in the root elongation zone and causes a temperature-sensitive defect in root elongation
-
-
?
acetyl-CoA + D-glucosamine 6-phosphate
CoA + N-acetyl-D-glucosamine 6-phosphate
-
-
-
?
acetyl-CoA + D-glucosamine 6-phosphate
CoA + N-acetyl-D-glucosamine 6-phosphate
-
-
-
?
acetyl-CoA + D-glucosamine 6-phosphate
CoA + N-acetyl-D-glucosamine 6-phosphate
-
-
-
?
acetyl-CoA + D-glucosamine 6-phosphate
CoA + N-acetyl-D-glucosamine 6-phosphate
-
-
-
?
acetyl-CoA + D-glucosamine 6-phosphate
CoA + N-acetyl-D-glucosamine 6-phosphate
-
-
-
-
?
acetyl-CoA + D-glucosamine 6-phosphate
CoA + N-acetyl-D-glucosamine 6-phosphate
-
-
-
?
acetyl-CoA + D-glucosamine 6-phosphate
CoA + N-acetyl-D-glucosamine 6-phosphate
-
-
-
?
acetyl-CoA + D-glucosamine 6-phosphate
CoA + N-acetyl-D-glucosamine 6-phosphate
-
-
-
?
acetyl-CoA + D-glucosamine 6-phosphate
CoA + N-acetyl-D-glucosamine 6-phosphate
-
-
-
?
acetyl-CoA + D-glucosamine 6-phosphate
CoA + N-acetyl-D-glucosamine 6-phosphate
-
highly specific for D-glucosamine-6-phosphate
-
?
propionyl-CoA + D-glucosamine 6-phosphate
CoA + N-propionyl-D-glucosamine 6-phosphate
-
-
-
?
propionyl-CoA + D-glucosamine 6-phosphate
CoA + N-propionyl-D-glucosamine 6-phosphate
-
15% of activity with acetyl-CoA
-
?
additional information
?
-
enzyme is not able to acetylate spermine or spermidine
-
-
-
additional information
?
-
enzyme is not able to acetylate spermine or spermidine
-
-
-
additional information
?
-
ratio of butanoyl-to-acetyltransferase activity for wild-type: 0.6. No substrates: isovaleryl-CoA and decanoyl-CoA
-
-
-
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G68S
-
the mutant called lignescens, a temperature-sensitive mutant that exhibits ectopic lignin deposition and growth defects under high-temperature conditions, is due to single base transition G68S in glucosamine-6-phosphate N-acetyltransferase. When exposed to the restrictive temperature, the mutant strain contains a significantly smaller amount of UDP-GlcNAc than the wild type. The growth defects and ectopic lignification of the mutant are suppressed by the addition of UDP-GlcNAc. N-glycans are reduced and luminal binding protein 3, a typical UPR gene, is expressed in the mutant strain at the restrictive temperature. Treatment with UPR-inducing reagents phenocopies the mutant
E185Y
-
Km (mM): 0.03 (D-glucosamine 6-phosphate), 0.04 (acetyl-CoA), kcat (1/sec): 1.34 (D-glucosamine 6-phosphate)
G183E
-
Km (mM): 0.056 (D-glucosamine 6-phosphate), 0.1 (acetyl-CoA), kcat (1/sec): 0.34 (D-glucosamine 6-phosphate)
V125R
-
Km (mM): 0.6 (D-glucosamine 6-phosphate), 0.2 (acetyl-CoA), kcat (1/sec): 0.12 (D-glucosamine 6-phosphate)
Y174F
-
crystal structure of the mutant Y174F acetyl-CoA/glucose-6-P complex is indistinguishable from the wild-type complex, mutant displays some remaining activity, kcat: 0.076/sec (glucosamine 6-phosphate)
Y189R
-
Km (mM): 0.056 (D-glucosamine 6-phosphate), 0.086 (acetyl-CoA), kcat (1/sec): 1.7 (D-glucosamine 6-phosphate)
Q155V/C158G
activity increases by 11.5% at pH 6.5-7.5, with the catalytic efficiency increasing by 27.5% to 1.25 per s and microM
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
biotechnology
-
engineering of a metabolic pathway for high level production of N-acetylglucosamine in Escherichia coli by overexpressing Escherichia coli glucosamine synthase (GlmS) and Saccharomyces cerevisiae glucosamine-6-phosphate acetyltransferase (GNA1)
additional information
-
mutation of the four nonconserved residues (V125, G183, E185 and Y189) lining the sugar-binding pocket suggests that they contribute to the kinetic differences between GNA1 from Aspergillus fumigatus and GNA1 from Homo sapiens
additional information
-
generation of a GlmU knockout strain discloses that GlmU is required for growth of Mycobacterium smegmatis as the bacteria does not grow in the absence of active GlmU enzyme
additional information
-
in a temperature shift experiment (from 30°C to 42°C) the amount of functional GlmU enzyme is gradually reduced the Mycobacterium smegmatis cells become non-viable and their morphology change from a normal rod shape to stubby-rounded morphology and in some cases they lyse
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Pattabiraman, T.N.; Bachhawat, B.K.
Purification of glucosamine-6-phosphate N-acetylase from sheep brain
Biochim. Biophys. Acta
59
681-689
1962
Ovis aries, Neurospora crassa
brenda
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, Oryctolagus cuniculus, Penicillium sp., Homo sapiens, Neurospora crassa, Streptococcus sp.
brenda
Davison, E.A.
Glucoseamine 6-phosphate N-acetylase
Methods Enzymol.
9
704-707
1966
Neurospora crassa, Neurospora crassa 5297a
-
brenda
Giddings, T.H.; Cantino, E.C.
Partial purification and properties of D-glucosamine 6-phosphate N-acetyltransferase from zoospores of Blastocladiella emersonii
J. Bacteriol.
120
976-979
1974
Blastocladiella emersonii
brenda
Corfield, A.P.; Mortimer, D.J.; Winterburn, P.J.
Purification and properties of acetyl-CoA: glucosamine-6-phosphate N-acetytransferase from rat liver
Biochem. Soc. Trans.
12
565
1984
Rattus norvegicus
-
brenda
Vessal, M.; Hassid, W.Z.
Partial purification and properties of D-glucosamine 6-phosphate N-acetyltransferase from Phaseolus aureus
Plant Physiol.
51
1055-1060
1973
Vigna radiata var. radiata
brenda
Porowski, T.S.; Porowska, H.; Galasinski, W.
Isolation, purification, and characterization of glucosamine-6-phosphate-N-acetylase from pig liver
Biochem. Med. Metab. Biol.
44
1-12
1990
Sus scrofa
brenda
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
-
brenda
Boehmelt, G.; Fialka, I.; Brothers, G.; McGinley, M.D.; Patterson, S.D.; Mo, R.; Hui, C.C.; Chung, S.; Huber, L.A.; Mak, T.W.; Iscove, N.N.
Cloning and characterization of the murine glucosamine-6-phosphate acetyltransferase EMeg32. Differential expression and intracellular membrane association
J. Biol. Chem.
275
12821-12832
2000
Mus musculus (Q9JK38), Mus musculus
brenda
Kato, N.; Mueller, C.R.; Wessely, V.; Lan, Q.; Christensen, B.M.
Mosquito glucosamine-6-phosphate N-acetyltransferase: cDNA, gene structure and enzyme kinetics
Insect Biochem. Mol. Biol.
35
637-646
2005
Aedes aegypti
brenda
Deng, M.D.; Severson, D.K.; Grund, A.D.; et al
Metabolic engineering of Escherichia coli for industrial production of glucosamine and N-acetylglucosamine
Metab. Eng.
7
201-214
2005
Arabidopsis thaliana, Saccharomyces cerevisiae, Candida albicans
brenda
Lopez, A.B.; Sener, K.; Jarroll, E.L.; van Keulen, H.
Transcription regulation is demonstrated for five key enzymes in Giardia intestinalis cyst wall polysaccharide biosynthesis
Mol. Biochem. Parasitol.
128
51-57
2003
Giardia intestinalis
brenda
Jiang, H.; Wang, S.; Dang, L.; Wang, S.; Chen, H.; Wu, Y.; Jiang, X.; Wu, P.
A novel short-root gene encodes a glucosamine-6-phosphate acetyltransferase required for maintaining normal root cell shape in rice
Plant Physiol.
138
232-242
2005
Oryza sativa
brenda
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
brenda
Deng, M.; Wassink, S.L.; Grund, A.D.
Engineering a new pathway for N-acetylglucosamine production: Coupling a catabolic enzyme, glucosamine-6-phosphate deaminase, with a biosynthetic enzyme, glucosamine-6-phosphate N-acetyltransferase
Enzyme Microb. Technol.
39
828-834
2006
Saccharomyces cerevisiae
-
brenda
Li, Y.; Lopez, P.; Durand, P.; Ouazzani, J.; Badet, B.; Badet-Denisot, M.A.
An enzyme-coupled assay for amidotransferase activity of glucosamine-6-phosphate synthase
Anal. Biochem.
370
142-146
2007
Saccharomyces cerevisiae
brenda
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)
brenda
Hurtado-Guerrero, R.; Raimi, O.; Shepherd, S.; van Aalten, D.M.
Glucose-6-phosphate as a probe for the glucosamine-6-phosphate N-acetyltransferase Michaelis complex
FEBS Lett.
581
5597-5600
2007
Aspergillus fumigatus
brenda
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
brenda
Zhang, W.; Jones, V.C.; Scherman, M.S.; Mahapatra, S.; Crick, D.; Bhamidi, S.; Xin, Y.; McNeil, M.R.; Ma, Y.
Expression, essentiality, and a microtiter plate assay for mycobacterial GlmU, the bifunctional glucosamine-1-phosphate acetyltransferase and N-acetylglucosamine-1-phosphate uridyltransferase
Int. J. Biochem. Cell Biol.
40
2560-2571
2008
Mycobacterium tuberculosis, Mycolicibacterium smegmatis
brenda
Riegler, H.; Herter, T.; Grishkovskaya, I.; Lude, A.; Ryngajllo, M.; Bolger, M.E.; Essigmann, B.; Usadel, B.
Crystal structure and functional characterization of a glucosamine-6-phosphate N-acetyltransferase from Arabidopsis thaliana
Biochem. J.
443
427-437
2012
Arabidopsis thaliana (Q9LFU9), Arabidopsis thaliana
brenda
Rodriguez-Diaz, J.; Rubio-Del-Campo, A.; Yebra, M.J.
Regulatory insights into the production of UDP-N-acetylglucosamine by Lactobacillus casei
Bioengineered
3
339-342
2012
Lacticaseibacillus casei
brenda
Rodriguez-Diaz, J.; Rubio-del-Campo, A.; Yebra, M.J.
Metabolic engineering of Lactobacillus casei for production of UDP-N-acetylglucosamine
Biotechnol. Bioeng.
109
1704-1712
2012
Lacticaseibacillus casei
brenda
Li, Y.; Zhou, Y.; Ma, Y.; Li, X.
Design and synthesis of novel cell wall inhibitors of Mycobacterium tuberculosis GlmM and GlmU
Carbohydr. Res.
346
1714-1720
2011
Mycobacterium tuberculosis
brenda
Sacoman, J.; Hollingsworth, R.
Synthesis and evaluation of an N-acetylglucosamine biosynthesis inhibitor
Carbohydr. Res.
346
2294-2299
2011
Bacillus subtilis, Escherichia coli
brenda
Marino, K.; Guether, M.L.; Wernimont, A.K.; Qiu, W.; Hui, R.; Ferguson, M.A.
Characterization, localization, essentiality, and high-resolution crystal structure of glucosamine 6-phosphate N-acetyltransferase from Trypanosoma brucei
Eukaryot. Cell
10
985-997
2011
Trypanosoma brucei (E3Q1H1), Trypanosoma brucei
brenda
Nozaki, M.; Sugiyama, M.; Duan, J.; Uematsu, H.; Genda, T.; Sato, Y.
A missense mutation in the glucosamine-6-phosphate N-acetyltransferase-encoding gene causes temperature-dependent growth defects and ectopic lignin deposition in Arabidopsis
Plant Cell
24
3366-3379
2012
Arabidopsis thaliana
brenda
Piacente, F.; Bernardi, C.; Marin, M.; Blanc, G.; Abergel, C.; Tonetti, M.G.
Characterization of a UDP-N-acetylglucosamine biosynthetic pathway encoded by the giant DNA virus Mimivirus
Glycobiology
24
51-61
2014
Mimivirus
brenda
Liu, Y.; Zhu, Y.; Ma, W.; Shin, H.D.; Li, J.; Liu, L.; Du, G.; Chen, J.
Spatial modulation of key pathway enzymes by DNA-guided scaffold system and respiration chain engineering for improved N-acetylglucosamine production by Bacillus subtilis
Metab. Eng.
24
61-69
2014
Bacillus subtilis, Bacillus subtilis BSGN4
brenda
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)
brenda
Ma, W.; Liu, Y.; Wang, Y.; Lv, X.; Li, J.; Du, G.; Liu, L.
Combinatorial fine-tuning of GNA1 and GlmS expression by 5-terminus fusion engineering leads to overproduction of N-acetylglucosamine in Bacillus subtilis
Biotechnol. J.
14
e1800264
2019
Caenorhabditis elegans (Q17427)
brenda
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)
-
brenda
Ma, W.; Liu, Y.; Lv, X.; Li, J.; Du, G.; Liu, L.
Combinatorial pathway enzyme engineering and host engineering overcomes pyruvate overflow and enhances overproduction of N-acetylglucosamine in Bacillus subtilis
Microb. Cell Fact.
18
001
2019
Caenorhabditis elegans (Q17427), Caenorhabditis elegans
brenda
Cova, M.; Lopez-Gutierrez, B.; Artigas-Jeronimo, S.; Gonzalez-Diaz, A.; Bandini, G.; Maere, S.; Carretero-Paulet, L.; Izquierdo, L.
The Apicomplexa-specific glucosamine-6-phosphate N-acetyltransferase gene family encodes a key enzyme for glycoconjugate synthesis with potential as therapeutic target
Sci. Rep.
8
4005
2018
Plasmodium falciparum (C6KTC5), Plasmodium falciparum, Cryptosporidium parvum (Q5CPU3), Toxoplasma gondii (S7UFV0), Toxoplasma gondii ATCC 50853 (S7UFV0), Cryptosporidium parvum Iowa II (Q5CPU3)
brenda