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Synonyms
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citrylglutamate synthase
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RIMKLB
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RIMKLB
gene name, ambiguous
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ATP + citrate + L-glutamate = ADP + phosphate + beta-citryl-L-glutamate
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citrate:L-glutamate ligase (ADP-forming)
The enzyme, found in animals, also has the activity of EC 6.3.2.41, N-acetylaspartylglutamate synthase.
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ADP + phosphate + beta-citryl-L-glutamate
ATP + citrate + L-glutamate
Substrates: isoform GCP3 acts preferentially on beta-citryl-L-glutamate in the presence of Ca2+. Its activity on this substrate is lower in the presence of Mn2+ and completely cancelled in the presence of Zn2+
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ADP + phosphate + N-acetyl-aspartylglutamate
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Substrates: in the presence of Ca2+, the purified enzyme specifically hydrolyzes beta-citrylglutamate and does not act on N-acetyl-aspartylglutamate. However, both compounds were hydrolyzed in the presence of Mn2+
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ATP + citrate + L-glutamate
ADP + phosphate + beta-citryl-L-glutamate
ATP + citrate + L-glutamate
ADP + phosphate + beta-citryl-L-glutamate
Substrates: -
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ATP + citrate + L-glutamate
ADP + phosphate + beta-citryl-L-glutamate
Substrates: the enzyme also has the activity of EC 6.3.2.41, N-acetylaspartylglutamate synthase. It catalyses the synthesis of beta-citryl-L-glutamate and N-acetyl-L-aspartyl-L-glutamate at nearly equal rates
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ATP + citrate + L-glutamate
ADP + phosphate + beta-citryl-L-glutamate
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Substrates: -
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ADP + phosphate + beta-citryl-L-glutamate
ATP + citrate + L-glutamate
Substrates: isoform GCP3 acts preferentially on beta-citryl-L-glutamate in the presence of Ca2+. Its activity on this substrate is lower in the presence of Mn2+ and completely cancelled in the presence of Zn2+
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ADP + phosphate + N-acetyl-aspartylglutamate
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Substrates: in the presence of Ca2+, the purified enzyme specifically hydrolyzes beta-citrylglutamate and does not act on N-acetyl-aspartylglutamate. However, both compounds were hydrolyzed in the presence of Mn2+
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ATP + citrate + L-glutamate
ADP + phosphate + beta-citryl-L-glutamate
ATP + citrate + L-glutamate
ADP + phosphate + beta-citryl-L-glutamate
Substrates: -
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ATP + citrate + L-glutamate
ADP + phosphate + beta-citryl-L-glutamate
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Substrates: -
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Ca2+
beta-citryl-L-glutamate is the preferred substrate in the presence of Ca2+
Mg2+
Mg2+ stimulates very poorly the activity of the enzyme
Mn2+
The N-acetyl-aspartylglutamate hydrolase activity of the enzyme is stimulated by Mn2+, but not by Ca2+
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dithiothreitol
stimulates
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Infertility, Male
Rimklb mutation causes male infertility in mice.
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0.0035
beta-Citryl-L-glutamate
in 25 mM HEPES, pH 7.1, at 30°C
1.24
citrate
pH 8.0, 30°C
0.73
L-glutamate
pH 8.0, 30°C
0.0076
N-acetyl-aspartylglutamate
in 25 mM HEPES, pH 7.1, at 30°C
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1.5
L-glutamate
pH 8.0, 30°C
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0.7
pH 8.0, 30°C, formation of beta-citryl-L-glutamate
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SwissProt
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brenda
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highest expression and activity
brenda
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brenda
Highest Expressing Human Cell Lines
Filter by:
Cell Line Links
Gene Links
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malfunction
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enzyme-deficient mice are impaired in a late step of spermiogenesis and produce spermatozoa with abnormally shaped heads and nuclei. Sperm chromatin in enzyme-deficient mice is less condensed and shows impaired histone to protamine exchange and retained transition protein 2
physiological function
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the enzyme is essential for efficient chromatin remodelling during spermiogenesis
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RIMKB_BOVIN
386
0
42550
Swiss-Prot
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RIMKB_DANRE
405
0
44500
Swiss-Prot
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RIMKB_MOUSE
387
0
42528
Swiss-Prot
other Location (Reliability: 3 )
RIMKB_HUMAN
386
0
42464
Swiss-Prot
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42000
x * 42000, SDS-PAGE
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Q-Sepharose column chromatography, ConA-Sepharose column chromatography, and Superdex S-200 gel filtration
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expressed in bacteria or HEK293T cells
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Collard, F.; Stroobant, V.; Lamosa, P.; Kapanda, C.N.; Lambert, D.M.; Muccioli, G.G.; Poupaert, J.H.; Opperdoes, F.; van Schaftingen, E.
Molecular identification of N-acetylaspartylglutamate synthase and beta-citrylglutamate synthase
J. Biol. Chem.
285
29826-29833
2010
Mus musculus (Q80WS1)
brenda
Collard, F.; Vertommen, D.; Constantinescu, S.; Buts, L.; Van Schaftingen, E.
Molecular identification of beta-citrylglutamate hydrolase as glutamate carboxypeptidase 3
J. Biol. Chem.
286
38220-38230
2011
Mus musculus (Q80WS1), Mus musculus
brenda
Wang-Eckhardt, L.; Sylvester, M.; Becker, I.; Allam, J.P.; Eckhardt, M.
Citrylglutamate synthase deficient male mice are subfertile with impaired histone and transition protein 2 removal in late spermatids
Biochem. J.
479
953-972
2022
Mus musculus
brenda
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