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Information on EC 6.3.2.11 - carnosine synthase and Organism(s) Homo sapiens and UniProt Accession A5YM72

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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:
Homo sapiens
UNIPROT: A5YM72
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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: Homo sapiens
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 synthase
-
carnosine synthase
-
-
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 + 4-aminobutanoate
AMP + phosphate + homocarnosine
show the reaction diagram
-
-
-
?
ATP + L-His + beta-Ala
ADP + phosphate + carnosine
show the reaction diagram
NATURAL SUBSTRATE
NATURAL 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 + beta-alanine
ADP + phosphate + carnosine
show the reaction diagram
-
-
-
?
ATP + L-His + beta-Ala
ADP + phosphate + carnosine
show the reaction diagram
-
the concentration of histidine in muscle and plasma is high relative to its Km with muscle carnosine synthase, whereas beta-alanine exists in low concentration in muscle and has a higher Km with muscle carnosine synthase, which indicates that it is the availability of beta-alanine that is limiting to the synthesis of carnosine in skeletal muscle
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
required
Co2+
-
activates
Mn2+
-
activates
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
dithiothreitol
-
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.84
4-aminobutanoate
pH 7.5, 37°C
0.42
ATP
pH 7.5, 37°C
0.09
beta-Alanine
pH 7.5, 37°C
0.37
L-histidine
pH 7.5, 37°C
4.67
L-lysine
pH 7.5, 37°C
7.66
L-ornithine
pH 7.5, 37°C
24.7
N-pi-methylhistidine
pH 7.5, 37°C
8.8
4-aminobutanoate
-
-
1.8
beta-Ala
-
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.05
4-aminobutanoate
pH 7.5, 37°C
0.003
ATP
pH 7.5, 37°C
1.28
beta-Alanine
pH 7.5, 37°C
0.004
L-histidine
pH 7.5, 37°C
0.0002
L-lysine
pH 7.5, 37°C
0.0001
L-ornithine
pH 7.5, 37°C
0.0001
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
primary kidney cells
Manually annotated by BRENDA team
primarily in proximal tubules, CARNS is expressed in glomeruli and tubular cells, close to the apical membrane
Manually annotated by BRENDA team
-
frontal and temporal cortex, activity decreases rapidly after brain death
Manually annotated by BRENDA team
additional information
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
histidine-containing dipeptides like carnosine and anserine have protective functions in both health and disease. Carnosine is synthesized by the enzyme carnosine synthase (CARNS), which is present in skeletal and heart muscle, as well as in certain regions in the brain and kidney
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
CRNS1_HUMAN
827
0
88484
Swiss-Prot
Secretory Pathway (Reliability: 5)
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
Kish, S.J.; Perry, T.L.; Hansen, S.
Regional distribution of homocarnosine, homocarnosine-carnosine synthetase and homocarnosinase in human brain
J. Neurochem.
32
1629-1636
1979
Homo sapiens
Manually annotated by BRENDA team
Bulygina, E.R.; Kramarenko, G.G.
Isolation of carnosine synthetase from animal and human muscles
Vopr. Med. Khim.
41
27-30
1995
Gallus gallus, Homo sapiens
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
Sale, C.; Saunders, B.; Harris, R.
Effect of beta-alanine supplementation on muscle carnosine concentrations and exercise performance
Amino Acids
39
321-333
2010
Homo sapiens
Manually annotated by BRENDA team
Peters, V.; Klessens, C.Q.; Baelde, H.J.; Singler, B.; Veraar, K.A.; Zutinic, A.; Drozak, J.; Zschocke, J.; Schmitt, C.P.; de Heer, E.
Intrinsic carnosine metabolism in the human kidney
Amino Acids
47
2541-2550
2015
Homo sapiens (A5YM72), Homo sapiens
Manually annotated by BRENDA team