Information on EC 5.4.2.10 -

Information on EC 5.4.2.10 - phosphoglucosamine mutase:

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EC NUMBER	COMMENTARY
5.4.2.10	-

RECOMMENDED NAME	GeneOntology No.
phosphoglucosamine mutase	GO:0008966

REACTION	REACTION DIAGRAM	COMMENTARY	ORGANISM	UNIPROT ACCESSION NO.	LITERATURE
alpha-D-glucosamine 1-phosphate = D-glucosamine 6-phosphate		The enzyme is involved in the pathway for bacterial cell-wall peptidoglycan and lipopolysaccharide biosynthesis, being an essential step in the pathway for UDP-N-acetylglucosamine biosynthesis. The enzyme from E. coli is activated by phosphorylation and can be autophosphorylated in vitro by glucosamine 1,6-bisphosphate, which is an intermediate in the reaction, glucose 1,6-bisphosphate or ATP. It can also catalyse the interconversion of glucose 1-phosphate and glucose 6-phosphate, although at a much lower rate	-	-	-

REACTION TYPE	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
isomerization	Bacillus anthracis	-	-	701529
isomerization	Streptococcus gordonii	-	-	703755
isomerization	Streptococcus mutans	Q8DTC6	-	706029
isomerization	-	-	intramolecular; intramolecular phosphate group transfer	-

PATHWAY	KEGG Link	MetaCyc Link
CMP-legionaminate biosynthesis	-	PWY-6749
UDP-N-acetyl-D-glucosamine biosynthesis I	-	UDPNAGSYN-PWY

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.

SYNONYMS	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
aminodeoxyglucose phosphate phosphomutase	-	-	-	-
GlmM	Streptococcus gordonii	-	-	692372, 703755, 716403
GlmM	Methanococcus maripaludis	Q6LYB4	-	692855
GlmM	Streptococcus mutans	Q8DTC6	-	706029
GlmM	Bacillus anthracis	Q81VN7	-	715384
glucosamine phosphomutase	-	-	-	-
MMP1077	Methanococcus maripaludis	Q6LYB4	-	692855
phosphoglucosamine mutase	Bacillus anthracis	-	-	701529
phosphoglucosamine mutase	Streptococcus gordonii	-	-	703755
phosphoglucosamine mutase	Streptococcus mutans	Q8DTC6	-	706029
PNGM	Bacillus anthracis	Q81VN7	-	715384

CAS REGISTRY NUMBER	COMMENTARY
9031-92-9	-

ORGANISM	COMMENTARY	LITERATURE	SEQUENCE CODE	SEQUENCE DB	SOURCE
Bacillus anthracis	-	701529	-	-
Bacillus anthracis	-	715384	Q81VN7	UniProt
Escherichia coli	-	210870, 210871, 210874	-	-
Geobacter sulfurreducens DL1	strain DL1	692372	A9CQM6	UniProt
Geobacter sulfurreducens DL1	strain DL1	703755	-	-
Helicobacter pylori	-	210873	-	-
Methanococcus maripaludis	strain 900	692855	Q6LYB4	UniProt
Methanococcus maripaludis 900	strain 900	692855	Q6LYB4	UniProt
Pseudomonas aeruginosa	-	210869	-	-
Staphylococcus aureus	-	210872	-	-
Streptococcus gordonii	-	716403	-	-
Streptococcus gordonii	strain DL1	692372	A9CQM6	UniProt
Streptococcus gordonii	strain DL1	703755	-	-
Streptococcus gordonii DL1	-	716403	-	-
Streptococcus mutans	strain UA159	706029	Q8DTC6	UniProt

GENERAL INFORMATION	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
malfunction	Streptococcus gordonii	-	glmM mutation causes marked elongation of the streptococcal chains, enlargement of bacterial cells, increased distortion of the bacterial cell surface, and defects in cell separation	716403
physiological function	Bacillus anthracis	-	phosphoglucosamine mutase catalyzes the conversion of glucosamine 6-phosphate to glucosamine 1-phosphate, an early step in the formation of the nucleotide sugar UDP-N-acetylglucosamine, which is involved in peptidoglycan biosynthesis	701529
physiological function	Streptococcus gordonii	-	phosphoglucosamine mutase catalyzes the interconversion of glucosamine 6-phosphate to glucosamine 1-phosphate, an essential step in the biosynthetic pathway leading to the formation of the peptidoglycan precursor uridine 5'-diphospho-N-acetylglucosamine	703755
physiological function	Streptococcus mutans	Q8DTC6	phosphoglucosamine mutase functions in the biosynthesis of peptidoglycan	706029
physiological function	Streptococcus gordonii	-	GlmM is involved in bacterial cell growth, morphology, biofilm formation, and sensitivity to penicillins	716403

SUBSTRATE	PRODUCT	REACTION DIAGRAM	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY/ Substrate	LITERATURE/ Substrate	COMMENTARY/ Product	LITERATURE/ Product	Reversibility r=reversible ir=irreversible ?=not specified
alpha-D-glucosamine 1-phosphate	D-glucosamine 6-phosphate		Streptococcus gordonii	-	-	703755	-	-	?
alpha-D-glucosamine 1-phosphate	D-glucosamine 6-phosphate		Bacillus anthracis	-	-	701529	-	-	?
alpha-D-glucosamine 1-phosphate	D-glucosamine 6-phosphate		Streptococcus mutans	Q8DTC6	-	706029	-	-	?
alpha-D-glucosamine 6-phosphate	alpha-D-glucosamine 1-phosphate		Methanococcus maripaludis	Q6LYB4	-	692855	-	-	r
alpha-D-glucose 1-phosphate	alpha-D-glucose 6-phosphate		Methanococcus maripaludis	Q6LYB4	-	692855	-	-	?
D-glucoamine 6-phosphate	D-glucosamine 1-phosphate		Escherichia coli	-	ping-pong bi-bi reaction mechanism	210870	-	210870	r
D-glucoamine 6-phosphate	D-glucosamine 1-phosphate		Escherichia coli	-	ping-pong bi-bi reaction mechanism, two basically different reaction sequences, 1. phosphate group transfer yielding the intermediate D-GlcN-1,6-diphosphate, 2. conversion to GlcN-1-phosphate	210871	-	210871	r
D-glucoamine 6-phosphate	D-glucosamine 1-phosphate		Staphylococcus aureus	-	involved in formation of cell-wall precursor UDP-N-acetylglucosamine	210872	-	210872	r
D-glucoamine 6-phosphate	D-glucosamine 1-phosphate		Escherichia coli	-	involved in formation of cell-wall precursor UDP-N-acetylglucosamine	210870	-	210870	r
D-glucoamine 6-phosphate	D-glucosamine 1-phosphate		Escherichia coli	-	involved in formation of cell-wall precursor UDP-N-acetylglucosamine	210871	-	210871	r
D-glucoamine 6-phosphate	D-glucosamine 1-phosphate		Escherichia coli	-	involved in formation of cell-wall precursor UDP-N-acetylglucosamine	210874	-	210874	r
D-glucoamine 6-phosphate	D-glucosamine 1-phosphate		Pseudomonas aeruginosa	-	involved in formation of cell-wall precursor UDP-N-acetylglucosamine	210869	-	210869	r
D-glucoamine 6-phosphate	D-glucosamine 1-phosphate		Helicobacter pylori	-	involved in formation of cell-wall precursor UDP-N-acetylglucosamine	210873	-	210873	r
D-glucosamine 1,6-diphosphate	D-glucosamine 6-phosphate		Escherichia coli	-	-	210871	-	210871	r
D-glucosamine 1-phosphate	D-glucosamine 6-phosphate		Escherichia coli	-	-	210871	-	210871	r
D-glucosamine 6-phosphate	D-glucosamine 1-phosphate		Streptococcus gordonii	-	-	716403	-	-	r
D-glucosamine 6-phosphate	D-glucosamine 1-phosphate		Streptococcus gordonii	A9CQM6	-	692372	-	-	r
D-glucosamine 6-phosphate	D-glucosamine 1-phosphate		Bacillus anthracis	Q81VN7	-	715384	-	-	r
D-glucose 1-phosphate	D-glucose 6-phosphate		Escherichia coli	-	in the presence of Glc-1,6-diphosphate, 1400fold lower activity than for D-glucosamine 1-phosphate or D-glucosamine 1,6-diphosphate, ping-pong reaction mechanism	210871	-	210871	?
D-glucose 1-phosphate	D-glucose 6-phosphate		Pseudomonas aeruginosa	-	50fold lower activity than phosphoglucosamine mutase activity	210869	-	210869	?
D-Mannose 1-phosphate	D-Mannose 6-phosphate		Pseudomonas aeruginosa	-	5fold lower activity than phosphoglucosamine mutase activity	210869	-	210869	?

NATURAL SUBSTRATES	NATURAL PRODUCTS	REACTION DIAGRAM	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY SUBSTRATE	LITERATURE (Substrate)	COMMENTARY PRODUCT	LITERATURE (Product)
alpha-D-glucosamine 1-phosphate	D-glucosamine 6-phosphate		Streptococcus gordonii	-	-	703755	-	-
alpha-D-glucosamine 1-phosphate	D-glucosamine 6-phosphate		Bacillus anthracis	-	-	701529	-	-
alpha-D-glucosamine 1-phosphate	D-glucosamine 6-phosphate		Streptococcus mutans	Q8DTC6	-	706029	-	-
D-glucoamine 6-phosphate	D-glucosamine 1-phosphate		Escherichia coli	-	ping-pong bi-bi reaction mechanism	210870	-	210870
D-glucoamine 6-phosphate	D-glucosamine 1-phosphate		Escherichia coli	-	ping-pong bi-bi reaction mechanism, two basically different reaction sequences, 1. phosphate group transfer yielding the intermediate D-GlcN-1,6-diphosphate, 2. conversion to GlcN-1-phosphate	210871	-	210871
D-glucoamine 6-phosphate	D-glucosamine 1-phosphate		Staphylococcus aureus	-	involved in formation of cell-wall precursor UDP-N-acetylglucosamine	210872	-	210872
D-glucoamine 6-phosphate	D-glucosamine 1-phosphate		Escherichia coli	-	involved in formation of cell-wall precursor UDP-N-acetylglucosamine	210870	-	210870
D-glucoamine 6-phosphate	D-glucosamine 1-phosphate		Escherichia coli	-	involved in formation of cell-wall precursor UDP-N-acetylglucosamine	210871	-	210871
D-glucoamine 6-phosphate	D-glucosamine 1-phosphate		Escherichia coli	-	involved in formation of cell-wall precursor UDP-N-acetylglucosamine	210874	-	210874
D-glucoamine 6-phosphate	D-glucosamine 1-phosphate		Pseudomonas aeruginosa	-	involved in formation of cell-wall precursor UDP-N-acetylglucosamine	210869	-	210869
D-glucoamine 6-phosphate	D-glucosamine 1-phosphate		Helicobacter pylori	-	involved in formation of cell-wall precursor UDP-N-acetylglucosamine	210873	-	210873
D-glucosamine 1,6-diphosphate	D-glucosamine 6-phosphate		Escherichia coli	-	-	210871	-	210871
D-glucosamine 1-phosphate	D-glucosamine 6-phosphate		Escherichia coli	-	-	210871	-	210871
D-glucosamine 6-phosphate	D-glucosamine 1-phosphate		Streptococcus gordonii	-	-	716403	-	-

COFACTOR	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE	IMAGE
No entries in this field

METALS and IONS	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
Mg2+	Escherichia coli	-	essential for autophosphorylation and catalytic activity	210870
Mg2+	Methanococcus maripaludis	Q6LYB4	activity is 95% lower when MgCl2 is used instead of MnCl2	692855
Mn2+	Methanococcus maripaludis	Q6LYB4	required for activity	692855

INHIBITORS	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE	IMAGE
Ca2+	Escherichia coli	-	80% reduced activity	210870	2D-image
EDTA	Escherichia coli	-	abolishes autophosphorylation and catalytic activity	210870	2D-image
Mn2+	Escherichia coli	-	80% reduced activity	210870	2D-image
Zn2+	Escherichia coli	-	efficient autophosphorylation, but absence of catalytic activity	210870	2D-image

ACTIVATING COMPOUND	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE	IMAGE
D-fructose-1,6-bisphosphate	Methanococcus maripaludis	Q6LYB4	required to activate the enzyme	692855	2D-image
D-glucosamine 1,6-diphosphate	Escherichia coli	-	retains the enzyme in an active and phosphorylated form	210870, 210871	2D-image
D-glucose 1,6-diphosphate	Escherichia coli	-	retains the enzyme in an active and phosphorylated form	210871	2D-image
D-glucose 1,6-diphosphate	Staphylococcus aureus	-	100fold activation	210872	2D-image
D-glucose 1,6-diphosphate	Escherichia coli	-	20fold activation at 0.7 mM	210874	2D-image
dithiothreitol	Methanococcus maripaludis	Q6LYB4	1 mM, required for maximal activity	692855	2D-image
additional information	Methanococcus maripaludis	Q6LYB4	no activity is observed with ATP as an activator	692855	-

KM VALUE [mM]	KM VALUE [mM] Maximum	SUBSTRATE	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE	IMAGE
0.08	-	D-glucosamine 1,6-diphosphate	Escherichia coli	-	-	210871	2D-image
0.08	-	D-glucosamine 1-phosphate	Escherichia coli	-	-	210871	2D-image
0.05	-	D-Glucosamine 6-phosphate	Escherichia coli	-	-	210871	2D-image
0.5	-	D-glucose 1,6-diphosphate	Escherichia coli	-	-	210871	2D-image
0.08	-	D-glucose 1-phosphate	Escherichia coli	-	single mutation S100T	210871	2D-image
0.65	-	D-glucose 1-phosphate	Escherichia coli	-	-	210871	2D-image

TURNOVER NUMBER [1/s]	TURNOVER NUMBER MAXIMUM[1/s]	SUBSTRATE	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE	IMAGE
0.52	-	alpha-D-glucosamine 1-phosphate	Methanococcus maripaludis	Q6LYB4	-	692855	2D-image
0.1	-	alpha-D-glucose 1-phosphate	Methanococcus maripaludis	Q6LYB4	-	692855	2D-image
2.42	-	D-Glucosamine 6-phosphate	Escherichia coli	-	6 x His-tagged recombinant enzyme	210871	2D-image
7.9	-	D-Glucosamine 6-phosphate	Escherichia coli	-	-	210871	2D-image
0.0055	-	D-glucose 1-phosphate	Escherichia coli	-	-	210871	2D-image
0.0138	-	D-glucose 1-phosphate	Escherichia coli	-	single-mutation S100T	210871	2D-image

kcat/KM VALUE [1/mMs^-1]	kcat/KM VALUE [1/mMs^-1] Maximum	SUBSTRATE	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE	IMAGE
No entries in this field

Ki VALUE [mM]	Ki VALUE [mM] Maximum	INHIBITOR	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE	IMAGE
No entries in this field

IC50 VALUE [mM]	IC50 VALUE [mM] Maximum	INHIBITOR	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE	IMAGE
No entries in this field

SPECIFIC ACTIVITY [µmol/min/mg]	SPECIFIC ACTIVITY MAXIMUM	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
0.007	-	Escherichia coli	-	substrate: D-glucose 6-phosphate	210871
0.06	-	Pseudomonas aeruginosa	-	substrate: D-glucose 1-phosphate	210869
0.1	-	Staphylococcus aureus	-	-	210872
0.55	-	Pseudomonas aeruginosa	-	substrate: D-mannose 1-phosphate	210869
0.95	-	Helicobacter pylori	-	-	210873
2.5	-	Pseudomonas aeruginosa	-	substrate: D-glucosamine 6-phosphate	210869
2.59	-	Escherichia coli	-	-	210874
3	-	Escherichia coli	-	6x His-tagged recombinant enzyme	210871
10	-	Escherichia coli	-	substrate: D-glucosamine 6-phosphate	210871

pH OPTIMUM	pH MAXIMUM	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
No entries in this field

pH RANGE	pH RANGE MAXIMUM	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
No entries in this field

TEMPERATURE OPTIMUM	TEMPERATURE OPTIMUM MAXIMUM	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
No entries in this field

TEMPERATURE RANGE	TEMPERATURE MAXIMUM	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
No entries in this field

pI VALUE	pI VALUE MAXIMUM	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
No entries in this field

SOURCE TISSUE	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE	SOURCE
cell culture	Escherichia coli	-	-	210870, 210871, 210874

LOCALIZATION	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	GeneOntology No.	LITERATURE	SOURCE
cytoplasm	Bacillus anthracis	-	-	5737	701529

PDB	SCOP	CATH	ORGANISM
3pdk, download	SCOP (3pdk)	CATH (3pdk)	Bacillus anthracis
3i3w, download	SCOP (3i3w)	CATH (3i3w)	Francisella tularensis subsp. tularensis (strain SCHU S4 / Schu 4)

MOLECULAR WEIGHT	MOLECULAR WEIGHT MAXIMUM	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
48370	-	Streptococcus gordonii	A9CQM6	calculated from amino acid sequence	692372
50000	-	Streptococcus gordonii	A9CQM6	His-tagged recombinant enzyme, SDS-PAGE	692372
50000	-	Methanococcus maripaludis	Q6LYB4	SDS-PAGE	692855
50960	-	Bacillus anthracis	-	-	701529
93100	-	Bacillus anthracis	Q81VN7	dynamic light scattering	715384
340000	-	Methanococcus maripaludis	Q6LYB4	gel filtration	692855

SUBUNITS	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
homodimer	Bacillus anthracis	Q81VN7	2 * 51000, X-ray crystallography	715384
trimer	Escherichia coli	-	3 * 47412, gel filtration, mass spectrometry	210871

POSTTRANSLATIONAL MODIFICATION	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
phosphoprotein	Escherichia coli	-	in vitro autophosphorylation at S102 in the presence of [gamma-32P]ATP	210870
phosphoprotein	Escherichia coli	-	the only phosphogroup at Ser102	210871
phosphoprotein	Escherichia coli	-	-	210874

Crystallization/COMMENTARY	ORGANISM	UNIPROT ACCESSION NO.	LITERATURE
the crystal structure of Bacillus anthracis phosphoglucosamine mutase is determined to a resolution of 2.7 A	Bacillus anthracis	-	701529

pH STABILITY	pH STABILITY MAXIMUM	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
No entries in this field

TEMPERATURE STABILITY	TEMPERATURE STABILITY MAXIMUM	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
No entries in this field

GENERAL STABILITY	ORGANISM	UNIPROT ACCESSION NO.	LITERATURE
No entries in this field

ORGANIC SOLVENT	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
No entries in this field

OXIDATION STABILITY	ORGANISM	UNIPROT ACCESSION NO.	LITERATURE
No entries in this field

STORAGE STABILITY	ORGANISM	UNIPROT ACCESSION NO.	LITERATURE
No entries in this field

Purification/COMMENTARY	ORGANISM	UNIPROT ACCESSION NO.	LITERATURE
using His-Select Ni-Affinity gel	Bacillus anthracis	-	701529
near homogeneity	Escherichia coli	-	210874
near homogeneity, recombinant enzyme	Escherichia coli	-	210870
near homogeneity; near homogeneity, recombinant enzyme	Escherichia coli	-	210871
near homogeneity, recombinant enzyme	Helicobacter pylori	-	210873
Ni+ affinity column chromatography	Methanococcus maripaludis	Q6LYB4	692855
near homogeneity, recombinant enzyme	Pseudomonas aeruginosa	-	210869
to homogeneity, recombinant enzyme	Staphylococcus aureus	-	210872
-	Streptococcus gordonii	A9CQM6	692372

Cloned/COMMENTARY	ORGANISM	UNIPROT ACCESSION NO.	LITERATURE
into the pDONR221 vector and subsequently into the pDEST17 vector for expression in Escherichia coli BL21DE3 cells	Bacillus anthracis	-	701529
overexpression in Escherichia coli	Escherichia coli	-	210870, 210871, 210874
overexpression in Escherichia coli	Helicobacter pylori	-	210873
expressed in Escherichia coli BL21(DE3) cells	Methanococcus maripaludis	Q6LYB4	692855
overexpression in Escherichia coli	Pseudomonas aeruginosa	-	210869
overexpression in Escherichia coli	Staphylococcus aureus	-	210872
expressed in Escherichia coli BL21 Star (DE3) cells	Streptococcus gordonii	A9CQM6	692372
into the pFW5 (Spec_r) Escherichia coli - streptococcus shuttle plasmid to create the mutant glmM gene, into the shuttle vector pDL289 to complement the glmM-deficient mutant strain	Streptococcus mutans	Q8DTC6	706029

EXPRESSION	ORGANISM	UNIPROT ACCESSION NO.	LITERATURE
a glmM-deficient Streptococcus mutans strain is used	Streptococcus mutans	Q8DTC6	706029

ENGINEERING	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
S100A	Escherichia coli	-	50fold less active	210870
S100A	Escherichia coli	-	very low activity	210871
S100T	Escherichia coli	-	contributes to the specificity towards sugar- or aminosugar-phosphates, much more efficient in catalysis of the phosphoglucose mutase reaction	210871
S102A	Escherichia coli	-	completely inactive, loss of autophosphorylation ability	210870
S102A	Escherichia coli	-	site of phosphorylation, no activity	210871
glmM mutant	Streptococcus gordonii	-	mutation resulted in increased sensitivity to polymorphonuclear leukocyte, PMN, -dependent killing, mutant induces increased superoxide anion production and lysozyme release by PMNs, mutant is more sensitive to lysozyme	703755
glmM mutant	Streptococcus mutans	Q8DTC6	mutant shows an altered general phenotype, reduced growth rate and increased autolysis, mutation results in defect biofilm formation	706029

Renatured/COMMENTARY	ORGANISM	UNIPROT ACCESSION NO.	LITERATURE
No entries in this field

APPLICATION	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
medicine	Streptococcus gordonii	-	phosphoglucosamine mutase could be a a novel drug target	703755
medicine	Streptococcus mutans	Q8DTC6	the glmM gene may have a constructive role in the virulence properties of Streptococcus mutans	706029

REF.	AUTHORS	TITLE	JOURNAL	VOL.	PAGES	YEAR	ORGANISM	LINK TO PUBMED	SOURCE
210869	Tavares, I.M.; Jolly, L.; Pompeo, F.; Leitao, J.H.; Fialho, A.M.; Sa-Correia, I.; Mengin-Lecreulx, D.	Identification of the Pseudomonas aeruginosa glmM gene, encoding phosphoglucosamine mutase	J. Bacteriol.	182	4453-4457	2000	Pseudomonas aeruginosa	PubMed
210870	Jolly, L.; Pompeo, F.; van Heijenoort, J.; Fassy, F.; Mengin-Lecreulx, D.	Autophosphorylation of phosphoglucosamine mutase from Escherichia coli	J. Bacteriol.	182	1280-1285	2000	Escherichia coli	PubMed
210871	Jolly, L.; Ferrari, P.; Blanot, D.; van Heijenoort, J.; Fassy, F.; Mengin-Lecreulx, D.	Reaction mechanism of phosphoglucosamine mutase from Escherichia coli	Eur. J. Biochem.	262	202-210	1999	Escherichia coli	PubMed
210872	Jolly, L.; Wu, S.; van Heijenoort, J.; De Lencastre, H.; Mengin-Lcreulx, D.; Tomasz, A.	The femR315 gene from Staphylococcus aureus, the interruption of which results in reduced methicillin resistance, encodes a phophoglucosamine mutase	J. Bacteriol.	179	5321-5325	1997	Staphylococcus aureus	PubMed
210873	De Reuse, H.; Labigne, A.; Mengin-Lecreulx, D.	The Helicobacter pylori ureC gene codes for a phosphoglucosamine mutase	J. Bacteriol.	179	3488-3493	1997	Helicobacter pylori	PubMed
210874	Mengin-Lecreulx, D.; van Heijenoort, J.	Characterization of the essential gene glmM encoding phosphoglucosamine mutase in Escherichia coli	J. Biol. Chem.	271	32-39	1996	Escherichia coli	PubMed
692372	Shimazu, K.; Takahashi, Y.; Uchikawa, Y.; Shimazu, Y.; Yajima, A.; Takashima, E.; Aoba, T.; Konishi, K.	Identification of the Streptococcus gordonii glmM gene encoding phosphoglucosamine mutase and its role in bacterial cell morphology, biofilm formation, and sensitivity to antibiotics	FEMS Immunol. Med. Microbiol.	53	166-177	2008	Streptococcus gordonii	PubMed
692855	Namboori, S.C.; Graham, D.E.	Acetamido sugar biosynthesis in the Euryarchaea	J. Bacteriol.	190	2987-2996	2008	Methanococcus maripaludis	PubMed
701529	Mehra-Chaudhary, R.; Neace, C.E.; Beamer, L.J.	Crystallization and initial crystallographic analysis of phosphoglucosamine mutase from Bacillus anthracis	Acta Crystallogr. Sect. F	65	733-735	2009	Bacillus anthracis	PubMed
703755	Yajima, A.; Takahashi, Y.; Shimazu, K.; Urano-Tashiro, Y.; Uchikawa, Y.; Karibe, H.; Konishi, K.	Contribution of phosphoglucosamine mutase to the resistance of Streptococcus gordonii DL1 to polymorphonuclear leukocyte killing	FEMS Microbiol. Lett.	297	196-202	2009	Streptococcus gordonii	PubMed
706029	Liu, X.D.; Duan, J.; Guo, L.H.	Role of phosphoglucosamine mutase on virulence properties of Streptococcus mutans	Oral Microbiol. Immunol.	24	272-277	2009	Streptococcus mutans	PubMed
715384	Mehra-Chaudhary, R.; Mick, J.; Beamer, L.J.	Crystal structure of phosphoglucosamine mutase from B. anthracis, an enzyme in the peptidoglycan biosynthetic pathway	J. Bacteriol.	193	4081-4087	2011	Bacillus anthracis	PubMed
716403	Shimazu, K.; Takahashi, Y.; Karibe, H.; Mitsuhashi, F.; Konishi, K.	Contribution of phosphoglucosamine mutase to determination of bacterial cell morphology in Streptococcus gordonii	Odontology	100	28-33	2012	Streptococcus gordonii	PubMed

LINKS TO OTHER DATABASES (specific for EC-Number 5.4.2.10)

NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM

IUBMB Enzyme Nomenclature

PROSITE Database of protein families and domains

SYSTERS

Protein Mutant Database

InterPro (database of protein families, domains and functional sites)

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