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

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Mark a special word or phrase in this record:
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)


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 ACCESSION NO.
LITERATURE
beta-alanyl-CoA = acryloyl-CoA + NH3
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
addition
-
-
of NH3
-
PATHWAY
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 ACCESSION NO.
COMMENTARY
LITERATURE
ammonia-lyase, beta-alanyl coenzyme A
-
-
-
-
beta-alanyl coenzyme A ammonia-lyase
-
-
-
-
beta-alanyl-CoA:ammonia lyase 2
Q6KC22
-
CAS REGISTRY NUMBER
COMMENTARY
9024-29-7
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
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 ACCESSION NO.
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 ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
NH4+
-, Q6KC22
100 mM, 70% inhibition of NH3 elimination
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
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]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
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]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
1033
-
-, Q6KC22
-
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
75000
-
-, Q6KC22
gel filtration
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
pentamer
-, Q6KC22
5 * 15999, MALDI-TOF MS
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE