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 hide
4.3.1.6
-
RECOMMENDED NAME
GeneOntology No.
beta-alanyl-CoA ammonia-lyase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
beta-alanyl-CoA = acryloyl-CoA + NH3
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
addition
-
-
of NH3
-
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.
CAS REGISTRY NUMBER
COMMENTARY hide
9024-29-7
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
acryloyl-CoA + NH3
beta-alanyl-CoA
show the reaction diagram
-
-
-
r
acrylyl-CoA + NH3
beta-alanyl-CoA
show the reaction diagram
-
-
-
ir
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
additional information
?
-
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NH4+
100 mM, 70% inhibition of NH3 elimination
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.023
acryloyl-CoA
pH 7.5
0.21
beta-alanyl-CoA
pH 7.0
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
195
acryloyl-CoA
Clostridium propionicum
Q6KC22
pH 7.5
25
beta-alanyl-CoA
Clostridium propionicum
Q6KC22
pH 7.0
301
NH3
Clostridium propionicum
Q6KC22
pH 7.5
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
75000
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homohexamer
three dimers combine to a homohexamer
pentamer
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
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE