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Literature summary for 2.7.3.13 extracted from

  • Taylor, Z.W.; Chamberlain, A.R.; Raushel, F.M.
    Substrate specificity and chemical mechanism for the reaction catalyzed by glutamine kinase (2018), Biochemistry, 57, 5447-5455 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.7.3.13

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli Rosetta (DE3) cells Campylobacter jejuni

Protein Variants

Protein Variants Comment Organism
H737N inactive Campylobacter jejuni

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.64
-
 L-glutamine at pH 8.0 and 25°C Campylobacter jejuni
1.5
-
 gamma-L-glutamyl hydroxamate at pH 8.0 and 25°C Campylobacter jejuni
10.5
-
 D-glutamine at pH 8.0 and 25°C Campylobacter jejuni
17.2
-
 gamma-L-glutamyl hydrazide at pH 8.0 and 25°C Campylobacter jejuni

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + L-glutamine + H2O Campylobacter jejuni
-
 AMP + phosphate + N5-phospho-L-glutamine
-
 r
ATP + L-glutamine + H2O Campylobacter jejuni ATCC 700819
-
 AMP + phosphate + N5-phospho-L-glutamine
-
 r

Organism

Organism UniProt Comment Textmining
Campylobacter jejuni Q0P8J6
-
-
Campylobacter jejuni ATCC 700819 Q0P8J6
-
-

Purification (Commentary)

Purification (Comment) Organism
HisTrap column chromatography and Sephadex gel filtration Campylobacter jejuni

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + beta-L-aspartyl hydroxamate + H2O
-
 Campylobacter jejuni AMP + phosphate + N5-phospho-beta-L-aspartyl hydroxamate
-
 ?
ATP + beta-L-aspartyl hydroxamate + H2O
-
 Campylobacter jejuni ATCC 700819 AMP + phosphate + N5-phospho-beta-L-aspartyl hydroxamate
-
 ?
ATP + D-glutamine + H2O
-
 Campylobacter jejuni AMP + phosphate + N5-phospho-D-glutamine
-
 ?
ATP + D-glutamine + H2O
-
 Campylobacter jejuni ATCC 700819 AMP + phosphate + N5-phospho-D-glutamine
-
 ?
ATP + gamma-L-glutamyl hydrazide + H2O
-
 Campylobacter jejuni AMP + phosphate + N5-phospho-gamma-L-glutamyl hydrazide
-
 ?
ATP + gamma-L-glutamyl hydroxamate + H2O second best substrate Campylobacter jejuni AMP + phosphate + N5-phospho-gamma-L-glutamyl hydroxamate
-
 ?
ATP + L-glutamine + H2O
-
 Campylobacter jejuni AMP + phosphate + N5-phospho-L-glutamine
-
 r
ATP + L-glutamine + H2O best substrate Campylobacter jejuni AMP + phosphate + N5-phospho-L-glutamine
-
 r
ATP + L-glutamine + H2O
-
 Campylobacter jejuni ATCC 700819 AMP + phosphate + N5-phospho-L-glutamine
-
 r
ATP + L-glutamine + H2O best substrate Campylobacter jejuni ATCC 700819 AMP + phosphate + N5-phospho-L-glutamine
-
 r
additional information no activity with L-glutamate and L-asparagine Campylobacter jejuni ?
-
-
additional information no activity with L-glutamate and L-asparagine Campylobacter jejuni ATCC 700819 ?
-
-

Synonyms

Synonyms Comment Organism
Cj1418
-
 Campylobacter jejuni
L-glutamine kinase
-
 Campylobacter jejuni

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.41
-
 gamma-L-glutamyl hydrazide at pH 8.0 and 25°C Campylobacter jejuni
1.5
-
 D-glutamine at pH 8.0 and 25°C Campylobacter jejuni
2.1
-
 gamma-L-glutamyl hydroxamate at pH 8.0 and 25°C Campylobacter jejuni
2.5
-
 L-glutamine at pH 8.0 and 25°C Campylobacter jejuni

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
0.0012
-
 beta-L-aspartyl hydroxamate at pH 8.0 and 25°C Campylobacter jejuni
0.024
-
 gamma-L-glutamyl hydrazide at pH 8.0 and 25°C Campylobacter jejuni
0.14
-
 D-glutamine at pH 8.0 and 25°C Campylobacter jejuni
1.4
-
 gamma-L-glutamyl hydroxamate at pH 8.0 and 25°C Campylobacter jejuni
3.9
-
 L-glutamine at pH 8.0 and 25°C Campylobacter jejuni