Information on EC 1.2.1.54 - gamma-guanidinobutyraldehyde dehydrogenase

for references in articles please use BRENDA:EC1.2.1.54
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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota

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EC NUMBER
COMMENTARY hide
1.2.1.54
-
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RECOMMENDED NAME
GeneOntology No.
gamma-guanidinobutyraldehyde dehydrogenase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
4-guanidinobutanal + NAD+ + H2O = 4-guanidinobutanoate + NADH + 2 H+
show the reaction diagram
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
L-arginine degradation IX (arginine:pyruvate transaminase pathway)
-
-
L-arginine degradation VIII (arginine oxidase pathway)
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-
arginine metabolism
-
-
Arginine and proline metabolism
-
-
Metabolic pathways
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-
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SYSTEMATIC NAME
IUBMB Comments
4-guanidinobutanal:NAD+ 1-oxidoreductase
Involved in the degradation of arginine in Pseudomonas putida (cf. EC 1.2.1.19 aminobutyraldehyde dehydrogenase).
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CAS REGISTRY NUMBER
COMMENTARY hide
56831-75-5
-
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
inducible by 2-ketoarginine
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
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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
4-aminobutyraldehyde + NAD+
4-aminobutanoate + NADH
show the reaction diagram
-
-
-
-
?
4-guanidinobutanal + NAD+
4-guanidinobutanoate + NADH
show the reaction diagram
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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
4-guanidinobutanal + NAD+
4-guanidinobutanoate + NADH
show the reaction diagram
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
not NADP+
-
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-Carboxy-2'-hydroxy-5'-sulfoformazylbenzene
-
zincon
diethyldithiocarbamate
-
-
Ferron
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-
N-ethylmaleimide
-
-
o-phenanthroline
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-
p-chloromercuribenzoate
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-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.03
4-guanidinobutyraldehyde
-
-
0.025
gamma-aminobutyraldehyde
-
-
0.0034
gamma-guanidinobutyraldehyde
-
-
0.084 - 0.14
NAD+
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
49.73
-
-
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
9.5
-
-
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7 - 10
-
pH 7.0: about 20% of activity maximum, pH 10.0: about 80% of activity maximum
7.5 - 10
-
pH 7.5: about 20% of activity maximum, pH 10: about 70% of activity maximum
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
-
Manually annotated by BRENDA team
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
57000
-
2 * 57000, SDS-PAGE
83000
-
gel filtration
107000
-
gel filtration
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
-
2 * 57000, SDS-PAGE
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.7 - 8.6
-
highest stability, 0°C, 24 h, 25% loss of activity
288292
9
-
0°C, 24 h, 63% loss of activity
288292
10
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0°C, 24 h, 96% loss of activity
288292
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0 - 20
-
stable
30
-
10 min, 4% loss of activity
40
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15 min, pH 8.0, 70% loss of activity
60
-
rapidly inactivated above
80
-
10 min, complete inactivation
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
inactive in absence of 2-mercaptoethanol
-
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
1-13 days, 4°C, 25-90% loss of activity, partial reactivation by dithiothreitol and 2-mercaptoethanol
-
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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LINKS TO OTHER DATABASES (specific for EC-Number 1.2.1.54)
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)