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Information on EC 2.3.1.4 - glucosamine-phosphate N-acetyltransferase and Organism(s) Caenorhabditis elegans and UniProt Accession Q17427

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Caenorhabditis elegans
UNIPROT: Q17427 not found.
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Word Map
The taxonomic range for the selected organisms is: Caenorhabditis elegans
The enzyme appears in selected viruses and cellular organisms
Synonyms
glucosamine-6-phosphate n-acetyltransferase, glucosamine 6-phosphate n-acetyltransferase, glucosamine-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
acetyltransferase, glucosamine phosphate
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-
-
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aminodeoxyglucosephosphate acetyltransferase
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-
-
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D-glucosamine-6-P N-acetyltransferase
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-
-
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glucosamine 6-phosphate acetylase
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-
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glucosamine 6-phosphate N-acetyltransferase
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glucosamine phosphate acetyltransferase
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-
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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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-
-
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phosphoglucosamine N-acetylase
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-
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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
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-
-
?
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.122 - 0.139
D-glucosamine 6-phosphate
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
136 - 151
D-glucosamine 6-phosphate
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
980 - 1230
D-glucosamine 6-phosphate
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
GNA1_CAEEL
165
0
18459
Swiss-Prot
other Location (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 19400, SDS-PAGE, mutant Q155V/C158G and wild-type
dimer
and monomer, 2 * 19400, SDS-PAGE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
synthesis
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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)
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team