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EC Tree
IUBMB Comments The enzyme, characterized from the bacterium Campylobacter jejuni, is involved in formation of a unique O-methyl phosphoramidate modification on specific sugar residues within the bacterium's capsular polysaccharides.
The expected taxonomic range for this enzyme is: Campylobacter jejuni
Synonyms
Cj1418, L-glutamine kinase,
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Cj1418
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L-glutamine kinase
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ATP + L-glutamine + H2O = AMP + phosphate + N5-phospho-L-glutamine
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ATP:L-glutamine N5-phosphotransferase
The enzyme, characterized from the bacterium Campylobacter jejuni, is involved in formation of a unique O-methyl phosphoramidate modification on specific sugar residues within the bacterium's capsular polysaccharides.
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ATP + beta-L-aspartyl hydroxamate + H2O
AMP + phosphate + N5-phospho-beta-L-aspartyl hydroxamate
ATP + D-glutamine + H2O
AMP + phosphate + N5-phospho-D-glutamine
ATP + gamma-L-glutamyl hydrazide + H2O
AMP + phosphate + N5-phospho-gamma-L-glutamyl hydrazide
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?
ATP + gamma-L-glutamyl hydroxamate + H2O
AMP + phosphate + N5-phospho-gamma-L-glutamyl hydroxamate
second best substrate
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?
ATP + L-glutamine + H2O
AMP + phosphate + N5-phospho-L-glutamine
additional information
?
-
ATP + beta-L-aspartyl hydroxamate + H2O
AMP + phosphate + N5-phospho-beta-L-aspartyl hydroxamate
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-
-
?
ATP + beta-L-aspartyl hydroxamate + H2O
AMP + phosphate + N5-phospho-beta-L-aspartyl hydroxamate
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?
ATP + D-glutamine + H2O
AMP + phosphate + N5-phospho-D-glutamine
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?
ATP + D-glutamine + H2O
AMP + phosphate + N5-phospho-D-glutamine
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?
ATP + L-glutamine + H2O
AMP + phosphate + N5-phospho-L-glutamine
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?
ATP + L-glutamine + H2O
AMP + phosphate + N5-phospho-L-glutamine
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r
ATP + L-glutamine + H2O
AMP + phosphate + N5-phospho-L-glutamine
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r
ATP + L-glutamine + H2O
AMP + phosphate + N5-phospho-L-glutamine
best substrate
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r
ATP + L-glutamine + H2O
AMP + phosphate + N5-phospho-L-glutamine
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r
ATP + L-glutamine + H2O
AMP + phosphate + N5-phospho-L-glutamine
best substrate
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r
ATP + L-glutamine + H2O
AMP + phosphate + N5-phospho-L-glutamine
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?
additional information
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no activity with ammonia, L-glutamate, or L-asparagine
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?
additional information
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no activity with L-glutamate and L-asparagine
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additional information
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no activity with L-glutamate and L-asparagine
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additional information
?
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no activity with L-glutamate and L-asparagine
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additional information
?
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no activity with ammonia, L-glutamate, or L-asparagine
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?
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ATP + L-glutamine + H2O
AMP + phosphate + N5-phospho-L-glutamine
ATP + L-glutamine + H2O
AMP + phosphate + N5-phospho-L-glutamine
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?
ATP + L-glutamine + H2O
AMP + phosphate + N5-phospho-L-glutamine
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r
ATP + L-glutamine + H2O
AMP + phosphate + N5-phospho-L-glutamine
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r
ATP + L-glutamine + H2O
AMP + phosphate + N5-phospho-L-glutamine
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r
ATP + L-glutamine + H2O
AMP + phosphate + N5-phospho-L-glutamine
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?
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0.34
ATP
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at pH 8.0 and 30°C
10.5
D-glutamine
at pH 8.0 and 25ðC
17.2
gamma-L-glutamyl hydrazide
at pH 8.0 and 25ðC
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1.5
gamma-L-glutamyl hydroxamate
at pH 8.0 and 25ðC
0.64
L-glutamine
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at pH 8.0 and 30°C
0.64
L-glutamine
at pH 8.0 and 25ðC
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2.5
ATP
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at pH 8.0 and 30°C
1.5
D-glutamine
at pH 8.0 and 25ðC
0.41
gamma-L-glutamyl hydrazide
at pH 8.0 and 25ðC
-
2.1
gamma-L-glutamyl hydroxamate
at pH 8.0 and 25ðC
2.5
L-glutamine
at pH 8.0 and 25ðC
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7.4
ATP
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at pH 8.0 and 30°C
0.0012
beta-L-aspartyl hydroxamate
at pH 8.0 and 25ðC
0.14
D-glutamine
at pH 8.0 and 25ðC
0.024
gamma-L-glutamyl hydrazide
at pH 8.0 and 25ðC
-
1.4
gamma-L-glutamyl hydroxamate
at pH 8.0 and 25ðC
3.9
L-glutamine
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at pH 8.0 and 30°C
3.9
L-glutamine
at pH 8.0 and 25ðC
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UniProt
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UniProt
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metabolism
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the enzyme is required for the biosynthesis of the phosphoramidate group of O-methyl phosphoramidate
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GLKIN_CAMJE
Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC 11168)
779
0
90325
Swiss-Prot
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H737N
inactive
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HisTrap column chromatography and Sephadex gel filtration
Ni affinity column chromatography
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expressed in Escherichia coli Rosetta (DE3) cells
expressed in Escherichia coli Rosetta (DE3) cells
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expressed in Escherichia coli Rosetta (DE3) cells
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Taylor, Z.W.; Brown, H.A.; Narindoshvili, T.; Wenzel, C.Q.; Szymanski, C.M.; Holden, H.M.; Raushel, F.M.
Discovery of a glutamine kinase required for the biosynthesis of the O-methyl phosphoramidate modifications found in the capsular polysaccharides of Campylobacter jejuni
J. Am. Chem. Soc.
139
9463-9466
2017
Campylobacter jejuni, Campylobacter jejuni NCTC11168
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Taylor, Z.W.; Raushel, F.M.
Cytidine diphosphoramidate kinase an enzyme required for the biosynthesis of the O-methyl phosphoramidate modification in the capsular polysaccharides of Campylobacter jejuni
Biochemistry
57
2238-2244
2018
Campylobacter jejuni
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Taylor, Z.W.; Chamberlain, A.R.; Raushel, F.M.
Substrate specificity and chemical mechanism for the reaction catalyzed by glutamine kinase
Biochemistry
57
5447-5455
2018
Campylobacter jejuni (Q0P8J6), Campylobacter jejuni, Campylobacter jejuni ATCC 700819 (Q0P8J6)
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2.7.3.13 glutamine kinase
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