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Information on EC 6.3.2.11 - carnosine synthase and Organism(s) Mus musculus and UniProt Accession Q6ZPS2

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EC Tree
     6 Ligases
         6.3 Forming carbon-nitrogen bonds
             6.3.2 Acid—amino-acid ligases (peptide synthases)
                6.3.2.11 carnosine synthase
IUBMB Comments
This enzyme was thought to form AMP [1,2], but studies with highly purified enzyme proved that it forms ADP . Carnosine is a dipeptide that is present at high concentrations in skeletal muscle and the olfactory bulb of vertebrates . It is also found in the skeletal muscle of some invertebrates. The enzyme can also catalyse the formation of homocarnosine from 4-aminobutanoate and L-histidine, with much lower activity .
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This record set is specific for:
Mus musculus
UNIPROT: Q6ZPS2
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Word Map
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  • 6.3.2.11
  • dipeptide
  • olfactory
  • bulb
  • castration-resistant
  • high-intensity
  • histidine-containing
  • carnosine-related
The taxonomic range for the selected organisms is: Mus musculus
The enzyme appears in selected viruses and cellular organisms
Synonyms
carnosine synthase, carnosine synthetase, carns, atpgd1, homocarnosine-carnosine synthetase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Carnosine synthetase
-
-
-
-
Carnosine-anserine synthetase
-
-
-
-
Carnosine-homocarnosine synthetase
-
-
-
-
CAS
-
-
-
-
HCarn-Carn synthetase
-
-
-
-
Homocarnosine-carnosine synthetase
-
-
-
-
Synthetase, carnosine
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
carboxylic acid amide formation
-
-
-
-
carboxamide formation
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
L-histidine:beta-alanine ligase (ADP-forming)
This enzyme was thought to form AMP [1,2], but studies with highly purified enzyme proved that it forms ADP [4]. Carnosine is a dipeptide that is present at high concentrations in skeletal muscle and the olfactory bulb of vertebrates [3]. It is also found in the skeletal muscle of some invertebrates. The enzyme can also catalyse the formation of homocarnosine from 4-aminobutanoate and L-histidine, with much lower activity [4].
CAS REGISTRY NUMBER
COMMENTARY hide
9023-61-4
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + L-histidine + 4-aminobutanoate
ADP + phosphate + homocarnosine
show the reaction diagram
-
-
-
?
ATP + L-histidine + beta-alanine
ADP + phosphate + carnosine
show the reaction diagram
-
-
-
?
ATP + L-lysine + beta-alanine
ADP + phosphate + ?
show the reaction diagram
-
-
-
?
ATP + L-ornithine + beta-alanine
ADP + phosphate + ?
show the reaction diagram
-
-
-
?
ATP + N-pi-methylhistidine + beta-alanine
ADP + phosphate + ?
show the reaction diagram
-
-
-
?
ATP + L-His + 3-amino-n-butanoate
AMP + phosphate + beta-n-aminobutanoyl-L-His
show the reaction diagram
-
-
-
-
?
ATP + L-His + beta-Ala
ADP + phosphate + carnosine
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NAD+
-
required
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1-methylhistidine
-
synthesis of carnosine
3-methylhistidine
-
synthesis of carnosine
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
6.44
4-aminobutanoate
pH 7.5, 37°C
0.57
ATP
pH 7.5, 37°C
0.46
beta-Alanine
pH 7.5, 37°C
0.11
L-histidine
pH 7.5, 37°C
1.59
L-lysine
pH 7.5, 37°C
0.52
L-ornithine
pH 7.5, 37°C
4.51
N-pi-methylhistidine
pH 7.5, 37°C
0.0166 - 0.0185
L-His
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.07
4-aminobutanoate
pH 7.5, 37°C
0.002
ATP
pH 7.5, 37°C
1.16
beta-Alanine
pH 7.5, 37°C
0.01
L-histidine
pH 7.5, 37°C
0.0009
L-lysine
pH 7.5, 37°C
0.0066
L-ornithine
pH 7.5, 37°C
0.0003
N-pi-methylhistidine
pH 7.5, 37°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
-
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
CRNS1_MOUSE
827
0
89281
Swiss-Prot
Secretory Pathway (Reliability: 5)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
430000
gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in HEK-293T cells
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Horinishi, H.; Grillo, M.; Margolis, F.L.
Purification and characterization of carnosine synthetase from mouse olfactory bulbs
J. Neurochem.
31
909-919
1978
Mus musculus
Manually annotated by BRENDA team
Ng, R.H.; Marshall, F.D.
Distribution of homocarnosine-carnosine synthetase in tissues of rat, mouse, chick and frog
Comp. Biochem. Physiol. B
54
519-521
1976
Gallus gallus, Mus musculus, Lithobates pipiens, Rattus norvegicus
Manually annotated by BRENDA team
Harding, J.W.; OFallon, J.V.
The subcellular distribution of carnosine, carnosine synthetase, and carnosinase in mouse olfactory tissues
Brain Res.
173
99-109
1979
Mus musculus
Manually annotated by BRENDA team
Drozak, J.; Veiga-da-Cunha, M.; Vertommen, D.; Stroobant, V.; Van Schaftingen, E.
Molecular identification of carnosine synthase as ATP-grasp domain-containing protein 1 (ATPGD1)
J. Biol. Chem.
285
9346-9356
2010
Homo sapiens (A5YM72), Homo sapiens, Gallus gallus (D3KCC4), Gallus gallus, Mus musculus (Q6ZPS2), Mus musculus
Manually annotated by BRENDA team