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Information on EC 6.3.2.11 - carnosine synthase
for references in articles please use BRENDA:EC6.3.2.11
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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 .
The enzyme appears in viruses and cellular organisms
showSynonyms
carnosine synthase, carnosine synthetase, carns, atpgd1, homocarnosine-carnosine synthetase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
ATPGD1
carnosine synthase
Carnosine synthetase
Carnosine-anserine synthetase
Carnosine-homocarnosine synthetase
CAS
-
-
-
-
HCarn-Carn synthetase
-
-
-
-
Homocarnosine-carnosine synthetase
Synthetase, carnosine
-
-
-
-
Carnosine synthetase
-
-
-
-
Carnosine-anserine synthetase
-
-
-
-
Carnosine-homocarnosine synthetase
-
-
-
-
Homocarnosine-carnosine synthetase
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + L-histidine + beta-alanine = ADP + phosphate + carnosine
-
-
-
-
ATP + L-histidine + beta-alanine = ADP + phosphate + carnosine
intermediary formation of enzyme bound beta-Ala
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
carboxamide formation
-
-
-
-
carboxylic acid amide formation
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
MetaCyc
carnosine biosynthesis, homocarnosine biosynthesis
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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].
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CAS REGISTRY NUMBER
COMMENTARY
9023-61-4
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + 1,2,4-triazole-3-Ala + beta-Ala
AMP + phosphate + beta-Ala-1,2,4-triazole-3-alanine
-
Substrates: -
Products: -
Products: -
?
ATP + 1-methylhistidine + beta-Ala
AMP + phosphate + beta-Ala-1-methylhistidine
-
Substrates: -
Products: -
Products: -
?
ATP + 2,6-diaminopimelate + beta-Ala
AMP + phosphate + beta-Ala-2,6-diaminopimelate
-
Substrates: -
Products: -
Products: -
?
ATP + 2-imidazole-3-Ala + beta-Ala
AMP + phosphate + beta-Ala-2-imidazole-3-Ala
-
Substrates: -
Products: -
Products: -
?
ATP + 2-methyl-L-His + beta-Ala
AMP + phosphate + beta-Ala-2-methyl-L-His
-
Substrates: -
Products: i.e. ophidine
Products: i.e. ophidine
?
ATP + 3-methylhistidine + beta-Ala
AMP + phosphate + beta-Ala-3-methylhistidine
-
Substrates: -
Products: -
Products: -
?
ATP + 5-hydroxylysine + beta-Ala
AMP + phosphate + beta-Ala-5-hydroxylysine
-
Substrates: -
Products: -
Products: -
?
ATP + Arg + beta-Ala
AMP + phosphate + beta-Ala-Arg
-
Substrates: -
Products: -
Products: -
?
ATP + DL-2-amino-6-hydroxyoctanoate + beta-Ala
AMP + phosphate + beta-Ala-DL-2-amino-6-hydroxyoctanoate
-
Substrates: -
Products: -
Products: -
?
ATP + DL-His-DL-His + beta-Ala
AMP + phosphate + beta-Ala-DL-His-DL-His
-
Substrates: -
Products: -
Products: -
?
ATP + L-canavanine + beta-Ala
AMP + phosphate + beta-Ala-L-canavanine
-
Substrates: -
Products: -
Products: -
?
ATP + L-His + 2,3-diaminopropanoate
AMP + phosphate + 2,3-diaminopropanoyl-L-His
-
Substrates: -
Products: -
Products: -
?
ATP + L-His + 2,4-diaminobutanoate
AMP + phosphate + 2,4-diaminobutanoyl-L-His
-
Substrates: -
Products: -
Products: -
?
ATP + L-His + 3-aminoisobutanoate
AMP + phosphate + 3-aminoisobutanoyl-L-His
-
Substrates: -
Products: -
Products: -
?
ATP + L-His + 5-aminopentanoate
AMP + phosphate + 5-aminopentanoyl-L-His
-
Substrates: -
Products: -
Products: -
?
ATP + L-His + 6-aminooctanoate
AMP + phosphate + 6-aminooctanoyl-L-His
-
Substrates: -
Products: -
Products: -
?
ATP + Lys + beta-Ala
AMP + phosphate + beta-Ala-Lys
-
Substrates: -
Products: -
Products: -
?
ATP + Orn + beta-Ala
AMP + phosphate + beta-Ala-Orn
-
Substrates: -
Products: -
Products: -
?
CTP + L-His + beta-Ala
CMP + phosphate + carnosine
-
Substrates: -
Products: -
Products: -
?
ITP + L-His + 4-aminobutanoate
IMP + phosphate + homocarnosine
-
Substrates: -
Products: -
Products: -
?
L-histidine + beta-alanine + ATP
carnosine + AMP + diphosphate
-
Substrates: -
Products: -
Products: -
?
additional information
?
-
-
Substrates: ATP-diphosphate exchange
Products: -
Products: -
?
ATP + L-His + 3-amino-n-butanoate
AMP + phosphate + beta-n-aminobutanoyl-L-His
-
Substrates: -
Products: -
Products: -
?
ATP + L-His + 3-amino-n-butanoate
AMP + phosphate + beta-n-aminobutanoyl-L-His
-
Substrates: -
Products: -
Products: -
?
ATP + L-His + 4-aminobutanoate
AMP + phosphate + homocarnosine
-
Substrates: -
Products: -
Products: -
?
ATP + L-His + 4-aminobutanoate
AMP + phosphate + homocarnosine
-
Substrates: -
Products: -
Products: -
?
ATP + L-His + 4-aminobutanoate
AMP + phosphate + homocarnosine
-
Substrates: -
Products: -
Products: -
?
ATP + L-His + 4-aminobutanoate
AMP + phosphate + homocarnosine
-
Substrates: -
Products: -
Products: -
?
ATP + L-His + beta-Ala
ADP + phosphate + carnosine
-
Substrates: -
Products: -
Products: -
?
ATP + L-His + beta-Ala
ADP + phosphate + carnosine
-
Substrates: not r
Products: -
Products: -
?
ATP + L-His + beta-Ala
ADP + phosphate + carnosine
-
Substrates: -
Products: -
Products: -
?
ATP + L-His + beta-Ala
ADP + phosphate + carnosine
-
Substrates: 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
Products: -
Products: -
?
ATP + L-His + beta-Ala
ADP + phosphate + carnosine
-
Substrates: -
Products: -
Products: -
?
ATP + L-His + beta-Ala
ADP + phosphate + carnosine
-
Substrates: -
Products: -
Products: -
?
ATP + L-His + beta-Ala
ADP + phosphate + carnosine
-
Substrates: -
Products: -
Products: -
?
ATP + L-histidine + 4-aminobutanoate
ADP + phosphate + homocarnosine
Substrates: -
Products: -
Products: -
?
ATP + L-histidine + 4-aminobutanoate
ADP + phosphate + homocarnosine
Substrates: -
Products: -
Products: -
?
ATP + L-histidine + 4-aminobutanoate
ADP + phosphate + homocarnosine
Substrates: -
Products: -
Products: -
?
ATP + L-histidine + beta-alanine
ADP + phosphate + carnosine
Substrates: -
Products: -
Products: -
?
ATP + L-histidine + beta-alanine
ADP + phosphate + carnosine
Substrates: -
Products: -
Products: -
?
ATP + L-histidine + beta-alanine
ADP + phosphate + carnosine
-
Substrates: -
Products: -
Products: -
?
ATP + L-histidine + beta-alanine
ADP + phosphate + carnosine
Substrates: -
Products: -
Products: -
?
ATP + L-lysine + beta-alanine
ADP + phosphate + ?
Substrates: -
Products: -
Products: -
?
ATP + L-lysine + beta-alanine
ADP + phosphate + ?
Substrates: -
Products: -
Products: -
?
ATP + L-lysine + beta-alanine
ADP + phosphate + ?
Substrates: -
Products: -
Products: -
?
ATP + L-ornithine + beta-alanine
ADP + phosphate + ?
Substrates: -
Products: -
Products: -
?
ATP + L-ornithine + beta-alanine
ADP + phosphate + ?
Substrates: -
Products: -
Products: -
?
ATP + L-ornithine + beta-alanine
ADP + phosphate + ?
Substrates: -
Products: -
Products: -
?
ATP + N-pi-methylhistidine + beta-alanine
ADP + phosphate + ?
Substrates: -
Products: -
Products: -
?
ATP + N-pi-methylhistidine + beta-alanine
ADP + phosphate + ?
Substrates: -
Products: -
Products: -
?
ATP + N-pi-methylhistidine + beta-alanine
ADP + phosphate + ?
Substrates: -
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + L-His + beta-Ala
ADP + phosphate + carnosine
-
Substrates: 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
Products: -
Products: -
?
ATP + L-histidine + beta-alanine
ADP + phosphate + carnosine
Substrates: -
Products: -
Products: -
?
L-histidine + beta-alanine + ATP
carnosine + AMP + diphosphate
-
Substrates: -
Products: -
Products: -
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Co2+
Mg2+
Mn2+
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Adenomatous Polyposis Coli
Activation of Wnt/?-catenin signaling in a subpopulation of murine prostate luminal epithelial cells induces high grade prostate intraepithelial neoplasia.
carnosine synthase deficiency
Carnosine synthase deficiency is compatible with normal skeletal muscle and olfactory function but causes reduced olfactory sensitivity in aging mice.
Hyperglycemia
Possible role of L-carnosine in the regulation of blood glucose through controlling autonomic nerves.
Myocardial Ischemia
Cardiospecific Overexpression of ATPGD1 (Carnosine Synthase) Increases Histidine Dipeptide Levels and Prevents Myocardial Ischemia Reperfusion Injury.
Neoplasms
A Tumor-Specific Cascade Amplification Drug Release Nanoparticle for Overcoming Multidrug Resistance in Cancers.
Neoplasms
Single luminal epithelial progenitors can generate prostate organoids in culture.
Prostatic Neoplasms
A luminal epithelial stem cell that is a cell of origin for prostate cancer.
Prostatic Neoplasms
Single luminal epithelial progenitors can generate prostate organoids in culture.
Reperfusion Injury
Cardiospecific Overexpression of ATPGD1 (Carnosine Synthase) Increases Histidine Dipeptide Levels and Prevents Myocardial Ischemia Reperfusion Injury.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
activity in muscle is higher after exercise, which may lead to an increase of the L-carnosine levels in plasma
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.3 - 8.5
-
6.3: about 70% of maximal activity, 8.5: about 55% of maximal activity
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
primarily in proximal tubules, CARNS is expressed in glomeruli and tubular cells, close to the apical membrane
brenda
additional information
-
frontal and temporal cortex, activity decreases rapidly after brain death
brenda
-
carnosine synthetase shows a 50fold increase in activity between 2 and 15 days, with some evidence for decline in activity subsequent to 21 days
brenda
additional information
carnosine-synthesizing and carnosine-hydrolyzing enzymes are localized in distinct compartments in the nephron, enzyme localization study, overview
brenda
additional information
-
carnosine-synthesizing and carnosine-hydrolyzing enzymes are localized in distinct compartments in the nephron, enzyme localization study, overview
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
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
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). CRNS1_CHICK
930
0
100060
Swiss-Prot
other Location (Reliability: 1)
CRNS1_HUMAN
827
0
88484
Swiss-Prot
Secretory Pathway (Reliability: 5)
CRNS1_MOUSE
827
0
89281
Swiss-Prot
Secretory Pathway (Reliability: 5)
A0A291LM21_HUMAN
205
0
23359
TrEMBL
other Location (Reliability: 1)
A0A8B6GBM5_MYTGA
406
0
45601
TrEMBL
other Location (Reliability: 1)
A0A812BXB1_SEPPH
514
0
58121
TrEMBL
other Location (Reliability: 1)
A0A8B6BVU3_MYTGA
956
0
107439
TrEMBL
other Location (Reliability: 1)
A0A6J8AHJ4_MYTCO
925
0
103888
TrEMBL
other Location (Reliability: 1)
A0A6J8CQL1_MYTCO
458
0
51853
TrEMBL
other Location (Reliability: 2)
A0A6J8EVR9_MYTCO
866
0
97593
TrEMBL
other Location (Reliability: 2)
A0A8B6CWS5_MYTGA
437
0
49070
TrEMBL
other Location (Reliability: 5)
A0A6J8BY33_MYTCO
429
0
48237
TrEMBL
other Location (Reliability: 2)
A0A6J8C450_MYTCO
853
0
97004
TrEMBL
Secretory Pathway (Reliability: 2)
A0A6J8BFL8_MYTCO
424
0
47893
TrEMBL
other Location (Reliability: 2)
U3MG62_PIG
827
0
88611
TrEMBL
other Location (Reliability: 4)
A0A8B6FDZ4_MYTGA
1785
0
200478
TrEMBL
other Location (Reliability: 4)
A0A8B6FDZ4_MYTGA
1785
0
200478
TrEMBL
other Location (Reliability: 4)
A0A6J8B5R1_MYTCO
717
0
81725
TrEMBL
Mitochondrion (Reliability: 4)
A0A6J8AK17_MYTCO
952
0
106980
TrEMBL
other Location (Reliability: 1)
A0A8B6BVP6_MYTGA
940
0
105480
TrEMBL
other Location (Reliability: 1)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
most of the activity is lost upon freezing or upon dialysis with EDTA-treated cellophan tubing for several h at 0°C
-
pH 7.0, 25°C, 1 h, with crystalline ribonuclease, not significantly inactivated
-
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in HEK-293T cells
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Seely, J.E.; Marshall, F.D.
Inhibition of carnosine synthetase by spermidine
Pept. Antibiot. Biosynth. Funct. (Kleinkauf H. et al. eds. )
347-352
1982
Bos taurus, Gallus gallus, Rattus norvegicus
-
brenda
Seely, J.E.; Marshall, F.D.
Carnosine-synthetase inhibition by beta-alanine analogues
Life Sci.
30
1763-1768
1982
Gallus gallus, Rattus norvegicus
brenda
Wood, M.R.G.; Johnson, P.
Purification of carnosine synthetase from avian muscle by affinity chromatography and determination of its subunit structure
Biochim. Biophys. Acta
662
138-144
1981
Gallus gallus
brenda
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
brenda
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
brenda
Ng, R.H.; Marshall, F.D.
Regional and subcellular distribution of homocarnosine-carnosine synthetase in the central nervous system of rats
J. Neurochem.
30
187-190
1978
Rattus norvegicus
-
brenda
Ng, R.H.; Marshall, F.D.
Subcellular distribution and some properties of homocarnosine-carnosine synthetase from chick red blood cells
Comp. Biochem. Physiol. B
54
523-525
1976
Gallus gallus
brenda
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
brenda
Ng, R.H.; Marshall, F.D.
The effect of various agents in vitro on homocarnosine-carnosine synthetase from rat brain
Experientia
32
839-841
1976
Rattus norvegicus
brenda
Skaper, S.D.; Das, S.; Marshall, F.D.
Some properties of a homocarnosine-carnosine synthetase isolated from rat brain
J. Neurochem.
21
1429-1445
1973
Rattus norvegicus
brenda
Kalyankar, G.D.; Meister, A.
Carnosine synthetase (chick muscle)
Methods Enzymol.
17
102-105
1971
Gallus gallus
-
brenda
McManus, R.; Benson, M.S.
Studies on the formation of carnosine and anserine in pectoral muscle of the developing chick
Arch. Biochem. Biophys.
119
444-453
1967
Gallus gallus
brenda
Stenesh, J.J.; Winnick, T.
Carnosine-anserine synthetase of muscle. 4. Partial purification of the enzyme and further studies of beta-alanyl peptide synthesis
Biochem. J.
77
575-581
1960
Gallus gallus
brenda
Kalyankar, G.D.; Meister, A.
Enzymatic synthesis of carnosine and related beta-alanyl and gamma-aminobutyryl peptides
J. Biol. Chem.
234
3210-3218
1959
Gallus gallus
brenda
Crowe, M.J.; Pixley, S.K.
Monoclonal antibody to carnosine synthetase identifies a subpopulation of frog olfactory receptor neurons
Brain Res.
538
147-151
1991
Lithobates pipiens
brenda
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
brenda
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
brenda
Nagai, K.; Niijima, A.; Yamano, T.; Otani, H.; Okumra, N.; Tsuruoka, N.; Nakai, M.; Kiso, Y.
Possible role of L-carnosine in the regulation of blood glucose through controlling autonomic nerves
Exp. Biol. Med.
228
1138-1145
2003
Rattus norvegicus
brenda
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
brenda
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
brenda
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
brenda
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Release 2023.1 (January 2023)
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