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

for references in articles please use BRENDA:EC4.3.1.6
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The expected taxonomic range for this enzyme is: Anaerotignum propionicum

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EC NUMBER
COMMENTARY hide
4.3.1.6
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RECOMMENDED NAME
GeneOntology No.
beta-alanyl-CoA ammonia-lyase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
beta-alanyl-CoA = acryloyl-CoA + NH3
show the reaction diagram
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-
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-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
addition
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-
of NH3
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
beta-Alanine metabolism
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Propanoate metabolism
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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.
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CAS REGISTRY NUMBER
COMMENTARY hide
9024-29-7
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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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
?
-
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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
?
-
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NH4+
100 mM, 70% inhibition of NH3 elimination
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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
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
195
acryloyl-CoA
pH 7.5
25
beta-alanyl-CoA
pH 7.0
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
15999
5 * 15999, MALDI-TOF MS
75000
gel filtration
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homohexamer
three dimers combine to a homohexamer
pentamer
5 * 15999, MALDI-TOF MS
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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
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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LINKS TO OTHER DATABASES (specific for EC-Number 4.3.1.6)
ExplorEnz
ExPASy
KEGG
MetaCyc
SABIO-RK
NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM
IUBMB Enzyme Nomenclature
PROSITE Database of protein families and domains
InterPro (database of protein families, domains and functional sites)