Information on EC 4.3.1.6 - beta-alanyl-CoA ammonia-lyase

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The expected taxonomic range for this enzyme is: Clostridium propionicum

EC NUMBER
COMMENTARY
4.3.1.6
-
RECOMMENDED NAME
GeneOntology No.
beta-alanyl-CoA ammonia-lyase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
beta-alanyl-CoA = acryloyl-CoA + NH3
show the reaction diagram
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
beta-Alanine metabolism
-
-
Propanoate metabolism
-
-
SYSTEMATIC NAME
IUBMB Comments
beta-alanyl-CoA ammonia-lyase (acryloyl-CoA-forming)
The reaction has only been demonstrated in the direction of addition of ammonia.
SYNONYMS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ammonia-lyase, beta-alanyl coenzyme A
-
-
-
-
beta-alanyl coenzyme A ammonia-lyase
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
9024-29-7
-
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
acryloyl-CoA + NH3
beta-alanyl-CoA
show the reaction diagram
Q6KC22
-
-
-
r
acrylyl-CoA + NH3
beta-alanyl-CoA
show the reaction diagram
-
-
-
ir
additional information
?
-
-
the enzyme may play a role as precursor in the biosynthesis of beta-alanyl peptides such as anserine and carnosine
-
-
-
additional information
?
-
Q6KC22
enzyme is induced by beta-alanine. The enzyme is needed to bind acryloyl-CoA, in order to keep the toxic free form at a very low level
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
additional information
?
-
-
the enzyme may play a role as precursor in the biosynthesis of beta-alanyl peptides such as anserine and carnosine
-
-
-
additional information
?
-
Q6KC22
enzyme is induced by beta-alanine. The enzyme is needed to bind acryloyl-CoA, in order to keep the toxic free form at a very low level
-
-
-
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NH4+
Q6KC22
100 mM, 70% inhibition of NH3 elimination
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.023
acryloyl-CoA
Q6KC22
pH 7.5
0.21
beta-alanyl-CoA
Q6KC22
pH 7.0
70
NH3
Q6KC22
pH 7.5
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
195
acryloyl-CoA
Q6KC22
pH 7.5
25
beta-alanyl-CoA
Q6KC22
pH 7.0
301
NH3
Q6KC22
pH 7.5
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
75000
Q6KC22
gel filtration
664903
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
homohexamer
Q6KC22
three dimers combine to a homohexamer
pentamer
Q6KC22
5 * 15999, MALDI-TOF MS
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
crystal structure of Acl in its apo-form at a resolution of 0.97 A as well as in complex with CoA at a resolution of 1.59 A. The structures reveal that the enyzme belongs to a superfamily of proteins exhibiting a so called 'hot dog fold' which is characterized by a five-stranded antiparallel beta-sheet with a long alpha-helix packed against it
Q6KC22
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE