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Information on EC 6.3.2.11 - carnosine synthase and Organism(s) Gallus gallus and UniProt Accession D3KCC4

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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:
Gallus gallus
UNIPROT: D3KCC4
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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: Gallus gallus
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
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + L-histidine + beta-alanine = ADP + phosphate + carnosine
show the reaction diagram
intermediary formation of enzyme bound beta-Ala
-
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 + 1,2,4-triazole-3-Ala + beta-Ala
AMP + phosphate + beta-Ala-1,2,4-triazole-3-alanine
show the reaction diagram
ATP + 1-methylhistidine + beta-Ala
AMP + phosphate + beta-Ala-1-methylhistidine
show the reaction diagram
ATP + 2,6-diaminopimelate + beta-Ala
AMP + phosphate + beta-Ala-2,6-diaminopimelate
show the reaction diagram
-
-
-
?
ATP + 2-imidazole-3-Ala + beta-Ala
AMP + phosphate + beta-Ala-2-imidazole-3-Ala
show the reaction diagram
ATP + 2-methyl-L-His + beta-Ala
AMP + phosphate + beta-Ala-2-methyl-L-His
show the reaction diagram
-
-
i.e. ophidine
?
ATP + 3-methylhistidine + beta-Ala
AMP + phosphate + beta-Ala-3-methylhistidine
show the reaction diagram
ATP + 5-hydroxylysine + beta-Ala
AMP + phosphate + beta-Ala-5-hydroxylysine
show the reaction diagram
ATP + Arg + beta-Ala
AMP + phosphate + beta-Ala-Arg
show the reaction diagram
ATP + DL-2-amino-6-hydroxyoctanoate + beta-Ala
AMP + phosphate + beta-Ala-DL-2-amino-6-hydroxyoctanoate
show the reaction diagram
-
-
-
?
ATP + DL-His-DL-His + beta-Ala
AMP + phosphate + beta-Ala-DL-His-DL-His
show the reaction diagram
-
-
-
?
ATP + L-canavanine + beta-Ala
AMP + phosphate + beta-Ala-L-canavanine
show the reaction diagram
-
-
-
?
ATP + L-His + 2,3-diaminopropanoate
AMP + phosphate + 2,3-diaminopropanoyl-L-His
show the reaction diagram
-
-
-
-
?
ATP + L-His + 2,4-diaminobutanoate
AMP + phosphate + 2,4-diaminobutanoyl-L-His
show the reaction diagram
ATP + L-His + 3-aminoisobutanoate
AMP + phosphate + 3-aminoisobutanoyl-L-His
show the reaction diagram
ATP + L-His + 4-aminobutanoate
AMP + phosphate + homocarnosine
show the reaction diagram
ATP + L-His + 5-aminopentanoate
AMP + phosphate + 5-aminopentanoyl-L-His
show the reaction diagram
-
-
-
-
?
ATP + L-His + 6-aminooctanoate
AMP + phosphate + 6-aminooctanoyl-L-His
show the reaction diagram
-
-
-
-
?
ATP + L-His + beta-Ala
ADP + phosphate + carnosine
show the reaction diagram
ATP + Lys + beta-Ala
AMP + phosphate + beta-Ala-Lys
show the reaction diagram
ATP + Orn + beta-Ala
AMP + phosphate + beta-Ala-Orn
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NAD+
-
brain, not required by enzyme from other tissues
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Co2+
-
stimulates with lower efficiency than Mg2+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-Aminoethylphosphonic acid
-
weak
3-Aminopropane sulfonic acid
-
competitive with respect to beta-Ala
5-Aminopentanoate
-
no inhibition
diphosphate
-
-
Fe2+
-
weak
iodoacetamide
-
-
K+
-
10-100 mM, weak inhibition
Mo2+
-
weak
Ni2+
-
-
O-Phosphoethanolamine
-
weak
PCMB
-
-
spermidine
-
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.35
4-aminobutanoate
pH 7.5, 37°C
0.19
ATP
pH 7.5, 37°C
0.033
beta-Alanine
pH 7.5, 37°C
0.1
L-histidine
pH 7.5, 37°C
1.42
L-lysine
pH 7.5, 37°C
1.62
L-ornithine
pH 7.5, 37°C
0.39
N-pi-methylhistidine
pH 7.5, 37°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.44
4-aminobutanoate
pH 7.5, 37°C
0.032
ATP
pH 7.5, 37°C
6.03
beta-Alanine
pH 7.5, 37°C
0.055
L-histidine
pH 7.5, 37°C
0.004
L-lysine
pH 7.5, 37°C
0.0026
L-ornithine
pH 7.5, 37°C
0.015
N-pi-methylhistidine
pH 7.5, 37°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5
assay at
7.3
-
-
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
CRNS1_CHICK
930
0
100060
Swiss-Prot
other Location (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
100000
SDS-PAGE
119000
-
2 * 119000, SDS-PAGE
250000
-
gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 100000, SDS-PAGE
dimer
-
2 * 119000, SDS-PAGE
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 8
-
stable in the range
1000
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
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-10°C, as a lyophilized powder, 25% loss of activity
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
affinity chromatography
-
partial
-
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
-
Manually annotated by BRENDA team
Seely, J.E.; Marshall, F.D.
Carnosine-synthetase inhibition by beta-alanine analogues
Life Sci.
30
1763-1768
1982
Gallus gallus, Rattus norvegicus
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
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
Kalyankar, G.D.; Meister, A.
Carnosine synthetase (chick muscle)
Methods Enzymol.
17
102-105
1971
Gallus gallus
-
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
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