Information on EC 2.6.1.43 - aminolevulinate transaminase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY hide
2.6.1.43
-
RECOMMENDED NAME
GeneOntology No.
aminolevulinate transaminase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
5-aminolevulinate + pyruvate = 4,5-dioxopentanoate + L-alanine
show the reaction diagram
A pyridoxal-phosphate protein
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
amino group transfer
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Porphyrin and chlorophyll metabolism
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-
SYSTEMATIC NAME
IUBMB Comments
5-aminolevulinate:pyruvate aminotransferase
A pyridoxal-phosphate protein.
CAS REGISTRY NUMBER
COMMENTARY hide
9012-46-8
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
bovine
-
-
Manually annotated by BRENDA team
3100
-
-
Manually annotated by BRENDA team
3100
-
-
Manually annotated by BRENDA team
bajra
-
-
Manually annotated by BRENDA team
S-50
-
-
Manually annotated by BRENDA team
S-50
-
-
Manually annotated by BRENDA team
ATCC 15920
-
-
Manually annotated by BRENDA team
IFO 3140
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
AG83, WHO nomenclature MHOM/IN/83/AG83, promastigote form
-
-
Manually annotated by BRENDA team
Mus musculus C57BL/6J
strain C57BL/6J and DBA/2J
-
-
Manually annotated by BRENDA team
radish
-
-
Manually annotated by BRENDA team
Wistar
-
-
Manually annotated by BRENDA team
3059, S288C
-
-
Manually annotated by BRENDA team
3059, S288C
-
-
Manually annotated by BRENDA team
Tulahuen strain, Tul 2 stock
-
-
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
beta-alanine + 4,5-dioxopentanoate
5-aminolevulinate + malonic semialdehyde
show the reaction diagram
D-alanine + 4,5-dioxopentanoate
5-aminolevulinate + pyruvate
show the reaction diagram
-
3% of the activity with L-alanine
-
-
ir
delta-amino-n-valerate + 4,5-dioxopentanoate
5-aminolevulinate + 5-oxo-n-pentanoate
show the reaction diagram
DL-alanine + 4,5-dioxopentanoate
5-aminolevulinate + pyruvate
show the reaction diagram
-
89% of the activity with L-alanine
-
-
ir
epsilon-amino-n-caproate + 4,5-dioxopentanoate
5-aminolevulinate + 6-oxo-n-hexanoate
show the reaction diagram
gamma-amino-n-butyrate + 4,5-dioxopentanoate
5-aminolevulinate + succinic semialdehyde
show the reaction diagram
glycine + 4,5-dioxopentanoate
5-aminolevulinate + glyoxylate
show the reaction diagram
L-alanine + 4,5-dioxopentanoate
5-aminolevulinate + pyruvate
show the reaction diagram
L-arginine + 4,5-dioxopentanoate
5-aminolevulinate + 5-guanidino-2-oxopentanoate
show the reaction diagram
-
6.8% of the activity with L-alanine
-
-
ir
L-asparagine + 4,5-dioxopentanoate
5-aminolevulinate + 4-amino-2,4-dioxobutanoic acid
show the reaction diagram
-
74% of the activity with L-alanine
-
-
ir
L-aspartate + 4,5-dioxopentanoate
5-aminolevulinate + oxaloacetate
show the reaction diagram
L-glutamate + 4,5-dioxopentanoate
5-aminolevulinate + 2-oxoglutarate
show the reaction diagram
L-glutamine + 4,5-dioxopentanoate
5-aminolevulinate + 2-oxoglutaramate
show the reaction diagram
L-histidine + 4,5-dioxopentanoate
5-aminolevulinate + 3-(1H-imidazol-4-yl)-2-oxopropanoate
show the reaction diagram
-
74% of the activity with L-alanine
-
-
ir
L-lysine + 4,5-dioxopentanoate
5-aminolevulinate + 6-amino-2-oxohexanoate
show the reaction diagram
L-ornithine + 4,5-dioxopentanoate
5-aminolevulinate + 5-amino-2-oxopentanoate
show the reaction diagram
L-phenylalanine + 4,5-dioxopentanoate
phenylpyruvate + 5-aminolevulinate
show the reaction diagram
L-serine + 4,5-dioxopentanoate
5-aminolevulinate + 3-hydroxy-2-oxopropanoate
show the reaction diagram
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
L-alanine + 4,5-dioxopentanoate
5-aminolevulinate + pyruvate
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pyridoxal 5'-phosphate
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-oxoglutarate
4,5-Dioxopentanoate
5-aminolevulinate
acetyl acetone
-
-
amino-oxyacetic acid
benzoyl acetone
-
-
beta-Alanine
-
8% inhibition
beta-chloroalanine
-
-
beta-Iodopropionate
-
30% inhibition
cadaverine
-
14% inhibition
cysteine
-
90% inhibition
diacetyl
DL-dithiothreitol
-
-
ethyl acetoacetate
-
-
gabaculine
-
-
glyoxylic acid
homocysteine
-
-
hydroxylamine
-
-
imidazole
-
-
iodoacetate
Isonicotinic acid hydrazide
lysine
-
20% inhibition
methylglyoxal
ophthalaldehyde
-
-
ornithine
-
20% inhibition
oxaloacetic acid
p-chloromercuribenzoate
p-chloromercuric benzene sulfonate
-
-
Penicillamine
-
-
potassium cyanide
-
-
protoporphyrin
-
-
pyruvate
Pyruvic acid
-
-
Semicarbazide
-
-
succinate semialdehyde
succinic acid
-
-
Thioglycollate
-
74% inhibition
Tris-HCl
additional information
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Hemin
-
cytoplasmic isozyme, stimulates to 150% of the control
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0105 - 1.8
4,5-Dioxopentanoate
0.67 - 1.3
glyoxylate
0.00028 - 8
L-alanine
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.5
glyoxylate
-
pH 8.0, 37C
30 - 42
Hemin
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.0266
-
-
0.16
-
-
0.22
-
cytosolic isozyme
0.753
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.9
-
-
7 - 8
-
-
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20 - 80
-
3fold increase of activity from 37C to 60C
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.7 - 4.8
-
isoelectric focusing using Phast GEl IEF 3-9
4.8
-
isoelectrofocusing column 110 ml and Pharmalyte gradient pH 3-10 at 4C for 45 h
5
-
isoelectric focusing analysis, 2-dimensional gel electrophoresis
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
60260
-
gel filtration
63000
-
SDS-PAGE
72000
-
sedimentation equilibrium centrifugation, potassium phosphate buffer containing 4 M NaCl
78000
-
sedimentation equilibrium centrifugation, potassium phosphate buffer
82000
-
gel filtration
111000
-
gel filtration
126000
-
gel filtration
146000
-
SDS-PAGE
168000
-
gel filtration
190000
-
gel filtration
210000
225000
232000
-
gel filtration
238000
-
gel filtration
240000
245000
-
sucrose density gradient centrifugation
260000
-
cytoplasmic isozyme, gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hexamer
monomer
tetramer
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
crystallized as bright yellow needles
-
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
55
-
retains 75% activity after 1 h incubation
55 - 65
-
retains more than 90% maximum activity through 55-65C, beyond 65C activity decreases sharply
60
-
10 min, about 65% loss of activity
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
freezing and thawing does not affect activity
-
glutathione or beta-mercaptoethanol restores activity of aged enzyme preparations, optimally at 1.0 mM
-
proteolytic hydrolysis of the cytosolic isozyme generates an enzymatically more active form
-
purified enzyme is stable in 50 mM potassium buffer, pH 6.9, containing 10% glycerol, freezing and thawing does not affect activity significantly
-
repeated freezing and thawing causes inactivation
-
repeated freezing and thawing inactivates the enzyme, stability of the enzyme is enhanced by presence of 5% glycerol
-
stability is improved by 10-15% glycerol
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-15C, stable for 3 months
-
-15C, stable for several months
-
-20C, 5 mM potassium phosphate buffer, pH 7.6, 10% glycerol
-
-20C, can be stored for nearly 1 year without significant loss of enzyme activity
-
-20C, purified enzyme in 50 mM potassium phosphate buffer, pH 7.5, 10% glycerol, may be stored for at least 8 weeks without loss of either activity
-
-20C, remains stable for at least 1 month
-
-70C, stable for at least 2-3 months
-
0-5C, 50 mM potassium phosphate buffer, pH 7.5, 10% glycerol, stored for 2 weeks, little or none of each activity is lost
-
4C, 10-15% glycerol, 20% loss of activity after 5 days
-
4C, can be stored for at least 1 week without any significant loss of activity
-
4C, stored in ice for 3 months without any appreciable loss of enzyme activity
-
4C, unstable
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine