show all | hide all No of entries

Information on EC 5.4.2.10 - phosphoglucosamine mutase and Organism(s) Methanococcus maripaludis and UniProt Accession Q6LYB4

for references in articles please use BRENDA:EC5.4.2.10
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
     5 Isomerases
         5.4 Intramolecular transferases
             5.4.2 Phosphotransferases (phosphomutases)
                5.4.2.10 phosphoglucosamine mutase
IUBMB Comments
The enzyme is involved in the pathway for bacterial cell-wall peptidoglycan and lipopolysaccharide biosyntheses, being an essential step in the pathway for UDP-N-acetylglucosamine biosynthesis. The enzyme from Escherichia coli is activated by phosphorylation and can be autophosphorylated in vitro by alpha-D-glucosamine 1,6-bisphosphate, which is an intermediate in the reaction, alpha-D-glucose 1,6-bisphosphate or ATP. It can also catalyse the interconversion of alpha-D-glucose 1-phosphate and glucose 6-phosphate, although at a much lower rate.
Specify your search results
Select one or more organisms in this record:
This record set is specific for:
Methanococcus maripaludis
UNIPROT: Q6LYB4
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
The expected taxonomic range for this enzyme is: Bacteria, Archaea
The taxonomic range for the selected organisms is: Methanococcus maripaludis
Synonyms
mmp1077, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
aminodeoxyglucose phosphate phosphomutase
-
-
-
-
glucosamine phosphomutase
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
alpha-D-glucosamine 1,6-phosphomutase
The enzyme is involved in the pathway for bacterial cell-wall peptidoglycan and lipopolysaccharide biosyntheses, being an essential step in the pathway for UDP-N-acetylglucosamine biosynthesis. The enzyme from Escherichia coli is activated by phosphorylation and can be autophosphorylated in vitro by alpha-D-glucosamine 1,6-bisphosphate, which is an intermediate in the reaction, alpha-D-glucose 1,6-bisphosphate or ATP. It can also catalyse the interconversion of alpha-D-glucose 1-phosphate and glucose 6-phosphate, although at a much lower rate.
CAS REGISTRY NUMBER
COMMENTARY hide
9031-92-9
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
alpha-D-glucosamine 6-phosphate
alpha-D-glucosamine 1-phosphate
show the reaction diagram
-
-
-
r
alpha-D-glucose 1-phosphate
alpha-D-glucose 6-phosphate
show the reaction diagram
-
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
activity is 95% lower when MgCl2 is used instead of MnCl2
Mn2+
required for activity
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
D-fructose-1,6-bisphosphate
required to activate the enzyme
dithiothreitol
1 mM, required for maximal activity
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.52
alpha-D-glucosamine 1-phosphate
-
0.1
alpha-D-glucose 1-phosphate
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain 900
UniProt
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
340000
gel filtration
PURIFICATION/commentary
ORGANISM
UNIPROT
LITERATURE
Ni+ affinity column chromatography
CLONED/commentary
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Namboori, S.C.; Graham, D.E.
Acetamido sugar biosynthesis in the Euryarchaea
J. Bacteriol.
190
2987-2996
2008
Methanococcus maripaludis, Methanococcus maripaludis (Q6LYB4)
Manually annotated by BRENDA team
Select items on the left to see more content.