Information on EC 2.6.1.2 - alanine transaminase

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

EC NUMBER
COMMENTARY hide
2.6.1.2
-
RECOMMENDED NAME
GeneOntology No.
alanine transaminase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
L-alanine + 2-oxoglutarate = pyruvate + L-glutamate
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
amino group transfer
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
alanine metabolism
-
-
Alanine, aspartate and glutamate metabolism
-
-
anaerobic energy metabolism (invertebrates, cytosol)
-
-
Arginine biosynthesis
-
-
C4 and CAM-carbon fixation
-
-
C4 photosynthetic carbon assimilation cycle, NAD-ME type
-
-
C4 photosynthetic carbon assimilation cycle, PEPCK type
-
-
Carbon fixation in photosynthetic organisms
-
-
L-alanine biosynthesis II
-
-
L-alanine degradation II (to D-lactate)
-
-
L-alanine degradation III
-
-
Metabolic pathways
-
-
Microbial metabolism in diverse environments
-
-
SYSTEMATIC NAME
IUBMB Comments
L-alanine:2-oxoglutarate aminotransferase
A pyridoxal-phosphate protein. 2-Aminobutanoate can act slowly instead of alanine.
CAS REGISTRY NUMBER
COMMENTARY hide
9000-86-6
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
cultivar Bugang
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
dolphin
-
-
Manually annotated by BRENDA team
Leptosphaeria michotii
fungi
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
six isoforms with different pH-optima
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
strain PAO2
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
mollusca: bivalvia
-
-
Manually annotated by BRENDA team
tomato, 2 alanine aminotransferases, soluble and Triton X-100 extractable
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
soil fungus
-
-
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
2-oxoglutarate + 5-aminopentanoate
glutamate + 5-oxopentanoate
show the reaction diagram
-
121% of the activity with beta-alanine
-
?
2-oxoglutarate + 6-aminohexanoate
glutamate + 6-oxohexanoate
show the reaction diagram
-
8% of the activity with beta-alanine
-
?
2-oxoglutarate + DL-3-aminoisobutanoate
glutamate + 3-oxoisobutanoate
show the reaction diagram
-
51% of the activity with beta-alanine
-
?
4-aminobutanoate + 2-oxoglutarate
4-oxobutanoate + glutamate
show the reaction diagram
-
at 131% of the activity with beta-alanine
-
?
4-aminobutanoate + 2-oxoglutarate
4-oxobutanoate + L-glutamate
show the reaction diagram
-
-
-
?
aspartate + 2-oxoglutarate
malate + L-glutamate
show the reaction diagram
14% of activity with glutamate and pyruvate
-
?
aspartate + pyruvate
malate + alanine
show the reaction diagram
10% of activity with alanine and 2-oxoglutarate
-
?
beta-alanine + 2-oxoglutarate
malonic semialdehyde + L-glutamate
show the reaction diagram
-
-
-
?
beta-alanine + glyoxylic acid
malonic semialdehyde + glycine
show the reaction diagram
-
7% of the activity with 2-oxoglutarate
-
?
beta-alanine + pyruvate
malonic semialdehyde + alanine
show the reaction diagram
-
1% of the activity with 2-oxoglutarate
-
?
DL-alanine + 2-oxoglutarate
pyruvate + L-glutamate
show the reaction diagram
glycine + 2-oxoglutarate
glyoxylate + glutamate
show the reaction diagram
-
24% of activity with DL-alanine
-
?
glyoxylate + alanine
glycine + pyruvate
show the reaction diagram
glyoxylate + glutamate
glycine + 2-oxoglutarate
show the reaction diagram
glyoxylate + glutamine
glycine + 2-oxosuccinamate
show the reaction diagram
-
42% of activity with glutamate
-
?
glyoxylate + methionine
glycine + 4-methylsulfanyl-2-oxobutanoate
show the reaction diagram
-
37% of activity with glutamate
-
?
L-alanine + 2-oxobutyrate
pyruvate + 2-aminobutanoate
show the reaction diagram
-
10.2% of the activity with 2-oxoglutarate
-
?
L-alanine + 2-oxoglutarate
pyruvate + L-glutamate
show the reaction diagram
L-alanine + glyoxylate
pyruvate + glycine
show the reaction diagram
L-glutamate and L-alanine are by far the best amino-group donors
-
-
?
L-alanine + glyoxylate
pyruvate + L-glycine
show the reaction diagram
-
-
-
-
ir
L-aspartate + 2-oxoglutarate
2-oxobutan-1,4-dioate + L-glutamate
show the reaction diagram
L-erythrulose + ?
2-amino-1,3,4-butanetriol + ?
show the reaction diagram
-
-
-
-
?
L-glutamate + 2-oxobutyrate
2-oxoglutarate + 2-aminobutanoate
show the reaction diagram
-
32.4% of the activity with pyruvate
-
?
L-glutamate + glyoxylate
2-oxoglutaramate + glycine
show the reaction diagram
L-glutamate and L-alanine are by far the best amino-group donors
-
-
?
L-leucine + 2-oxoglutarate
2-oxo-4-methylpentanoate + L-glutamate
show the reaction diagram
L-methionine + 2-oxoglutarate
4-methylsulfanyl-2-oxobutanoate + L-glutamate
show the reaction diagram
-
75% of activity with DL-alanine
-
?
L-methylbenzylamine + 2-oxoglutarate
?
show the reaction diagram
-
-
-
-
?
L-tyrosine + 2-oxoglutarate
(4-hydroxyphenyl)pyruvate + L-glutamate
show the reaction diagram
-
12.5% specific activity compared to L-alanine
-
-
?
L-tyrosine + 2-oxoglutarate
2-deamino-2-oxotyrosine + L-glutamate
show the reaction diagram
-
12-14% of the activity with L-alanine
-
-
?
pyruvate + L-glutamate
L-alanine + 2-oxoglutarate
show the reaction diagram
-
-
-
r
serine + 2-oxoglutarate
3-hydroxy-2-oxopropanoate + glutamate
show the reaction diagram
-
22% of activity with DL-alanine
-
?
tyrosine + 2-oxoglutarate
3-(4-hydroxyphenyl)-2-oxopropanoate + glutamate
show the reaction diagram
-
36.5% of activity with DL-alanine
-
?
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 + 2-oxoglutarate
pyruvate + L-glutamate
show the reaction diagram
additional information
?
-
-
the acetylpolyamine amidohydrolase regulator alanine transaminase and racemase coupled with SpuC, the major putrescine-pyruvate transaminase, are key components to maintaining alanine homeostasis. The alanine-pyruvate cycle is indispensable for polyamine utilization, corresponding mutant strains are severely hampered in polyamine utilization, overview
-
-
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pyridoxal 5'-phosphate
additional information
-
anaerobically induced isoform does not require the presence of pyridoxal 5'-phosphate to retain its activity
-
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(aminooxy)acetate
1,10-phenanthroline
-
2 mM, 51% inhibition
2-oxoglutarate
-
substrate inhibition at neutral pH, not seen at pH 8.8
3-chloro-L-alanine
-
0.1 mM, 78% inhibition
4-hydroxymercuribenzoate
-
-
6-Azauracil
-
1.5 mM, 50% inhibition
acarbose
-
0.1% acarbose fed to diabetic mice induces a decrease of the catalytic activity to 69.6%
Ag+
-
-
Al3+
-
-
Aminooxyacetate
aminooxyacetic acid
-
2.5 mM, complete inhibition
Citric acid
-
-
Co2+
-
-
cycloserine
D-alanine
-
competitive vs. L-alanine
EDTA
-
-
Fumaric acid
-
-
Glutarate
hydroxylamine
Isonicotinic hydrazide
-
-
L-ascorbic acid
-
2 mM, 25% inhibition
malate
-
5 mM, 25% inhibition
Maleate
Maleic acid
-
-
o-phenanthroline
-
weak
oxalic acid
-
-
p-chloromercuribenzoate
p-hydroxymercuribenzoate
Phenelzine
-
monoamine oxidase inhibitor used as antidepressant/antipanic drug, maximum inhibition, i.e. 32%, of brain alanine aminotransferase at 15 mg/kg
phenylhydrazine
-
-
Semicarbazide
succinate
-
competitive inhibitor
vigabatrin
-
structural analogue to gamma-amino butyric acid, anti-epilepsy drug, 1 mM, approx. 80% inhibition in vitro, in vivo alanine aminotransferase activity is reduced 30-40% 1-2h after administration
additional information
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NH4+
-
ammonium as nitrogen source induces both gene expression and enzyme activity of AlaAT
additional information
-
an 1.5fold increase in enzyme activity is detected under hypoxic conditions
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0058 - 5
2-oxoglutarate
0.51
4-aminobutanoate
-
pH 8.8, 37C, cosubstrate 2-oxoglutarate
0.25 - 21
alanine
3.9 - 7.6
beta-Alanine
8.3
DL-alanine
-
pH 8.6, 37C
0.55 - 32
glutamate
0.75 - 0.9
glyoxylate
0.21 - 30.3
L-alanine
0.2 - 6.66
L-glutamate
0.022 - 5.6
pyruvate
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.08 - 170
2-oxoglutarate
0.33 - 170
L-alanine
0.17 - 136
L-glutamate
0.67 - 136
pyruvate
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
22290 - 24640
2-oxoglutarate
24640
L-alanine
Triticum aestivum
-
AlaAT2, cosubstrate: 2-oxoglutarate, pH 7.3, 25C
103
19630 - 20510
L-glutamate
20510
pyruvate
Triticum aestivum
-
AlaAT2, cosubstrate: L-glutamate, pH 7.3, 25C
31
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00034 - 0.00064
Aminooxyacetate
17
succinate
-
pH 8.6, 37C
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0069
(aminooxy)acetate
Hordeum vulgare
P52894
25C, pH 8.0
0.119
cycloserine
Hordeum vulgare
P52894
25C, pH 8.0
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.12
-
enzyme from cell lysate
0.75
substrate gamma-aminobutanoate, continuous assay with succinate dehydrogenase, pH 8.0, 30C
1.39
-
-
1.6
substrate gamma-aminobutanoate, continuous assay using malonic semialdehyde decarboxylase and alcohol dehydrogenase, pH 8.0, 30C
2.1
pH 7.4, 25C, L-alanine (10 mM) + glyoxylate
2.5
pH 7.4, 25C, L-glutamate (10 mM) + glyoxylate
3.52
substrate beta-alanine, discontinuous determination of glutamate using glutamate dehydrogenase in the presence of 10 M hydrazine, pH 8.0, 30C
3.55
-
-
4.5
substrate beta-alanine, continuous assay using malonic semialdehyde decarboxylase and alcohol dehydrogenase, pH 8.0, 30C
30.58
-
isoform AlaAT I
43.3
-
isoform AlaAT II
50
-
pH 7.4, 25C
60.2
-
25C
89.5
-
pH 7.4, 25C
127.5
-
-
156
-
reverse reaction
158
native enzyme
213
-
-
229.8
-
after purification
243
recombinant enzyme
360
Leptosphaeria michotii
-
-
594
-
forward reaction
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 7.5
-
-
6.5 - 7.5
-
forward and reverse reaction
6.5 - 7.8
native and recombinant enzyme
7.3
-
assay at
7.5 - 8.5
-
-
8 - 8.3
-
with alanine and 2-oxoglutarate
8.2
-
isoform in eggs
8.3
-
in borate buffer
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3.5 - 9.5
-
active over whole range
5.5 - 9.5
-
approx. 70% of maximal activity at pH 5.5, approx. 50% of maximal activity at pH 9.5
5.5 - 8.2
native and recombinant enzyme
6.3 - 7.8
-
approx. 40% of maximal activity at pH 6.3, 75% of maximal activity at pH 6.8
6.4 - 8.7
-
at least 50% of maximal activity at pH 6.4 and 8.7
6.5 - 8
-
almost full activity within this range
6.5 - 7.5
-
-
7 - 9
more than 70% of maximum activity
7 - 7.5
-
rapid decrease of activity below pH 7 and above pH 7.5
7.9 - 8.4
-
highest activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25 - 55
-
strong decrease above
30 - 95
native and recombinant enzyme
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.3
-
isoform AlaAT II, isoelectric focusing
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
three isoforms with different pH-optima
Manually annotated by BRENDA team
-
stroma
Manually annotated by BRENDA team
-
highest activity, two isoforms with different pH-optima
Manually annotated by BRENDA team
-
increase in alanine aminotransferase activity during lactation and weaning when compared to virgin rats
Manually annotated by BRENDA team
-
highest expression found
Manually annotated by BRENDA team
-
mitochondrial enzyme
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
17700
-
SDS-PAGE
18300
-
gel filtration
18370
-
isoform AlaAT I, gel filtration
53000
-
enzyme containing a His- and a T5-tag, SDS-PAGE
54820
-
calculated from sequence of cDNA
55100
-
LC mass spectrometry
57000
recombinant enzyme
57900
-
SDS-PAGE
61300
-
SDS-PAGE
80000
-
gel filtration
92000
-
-
93400
gel filtration
97000
-
gel filtration
99000
-
gel filtration
100000
-
gel filtration
101000
-
SDS-PAGE
102000
-
gel filtration
105000
-
gel filtration
110000
Leptosphaeria michotii
-
-
111000
gel filtration; PAGE
112000 - 118000
112000
-
sucrose density gradient centrifugation
114800
-
isoform AlaAT II, gel filtration
115000
-
gel filtration
118000
-
sucrose density gradient centrifugation
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
HvAlaAT is crystallized in complex with pyridoxal 5'-phosphate and L-cycloserine. Structure of this complex is solved at 2.7 A resolution
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5
-
strong loss of activity below
636720
7 - 9
70% of activity remaining at pH values of 7 and 9
673585
7.5
-
40C, 30 min, 50% loss of activity
636724
8.5 - 9.5
-
more stable at alkaline pH than at neutral pH
636724
9
-
40C, 30 min, 5% loss of activity
636724
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
22
-
isoenzymes 2 and 3, 10-20% loss of activity after 3 h
40
-
30 min, 50% loss of activity at pH 7.5, 5% loss of activity at pH 9.0
60
-
more than 85% loss of activity after 5 min
additional information
-
pyridoxal 5-phosphate, L-alanine or 2-oxoglutarate protect against heat inactivation
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
during the purification procedure the enzyme needs protective substances, i.e. glycerol, 2-mercaptoethanol and alanine
-
enzyme does not tolerate freezing at any stage after sonication of the isolated mitochondria
-
K+ or L-alanine stabilizes
-
pyridoxal 5'-phosphate, L-alanine or 2-oxoglutarate protects against heat inactivation
-
uneffected by repeated freezing and thawing
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, 10% glycerol, half-life of 2 weeks
-
-20C, 20 mM Tris-HCl, pH 7.5, freezing is worse than storage at 4C or 25C
-
-20C, 50 mM potassium phosphate buffer, pH 7.5, 5 mM 2-mercaptoethanol, 5% glycerol, stable for at least 5 weeks
-
-20C, stable for several months
-
-25C, 10 mM potassium phosphate, pH 7.5, 1 mM EDTA, 2 mM 2-mercaptoethanol, 0.04 mM pyridoxal 5'-phosphate, a few days, 50% loss of activity
-
-80C, 20 mM Tris-HCl, pH 7.5, 20% loss of activity in first two days, thereafter stable for at least 20 days. Addition of 25% glycerol preserves most of the activity
-
-80C, 20 mM Tris-HCl, pH 7.5, stable for at least 20 days. Addition of 25% glycerol preserves most of the activity
-
0-5C, 50 mM potassium phosphate buffer, pH 7.5, 5 mM 2-mercaptoethanol, 5% glycerol, stable for 2 weeks
-
0C, stable for several h in solution
-
25C, 20 mM Tris-HCl, pH 7.5, 56% loss of activity in first two days. Addition of 25% glycerol preserves most of the activity
-
25C, 20 mM Tris-HCl, pH 7.5, 80-90% residual activity after 10 days, 60% residual activity after 20 days. Addition of 25% glycerol preserves most of the activity
-
37C, 20 mM Tris-HCl, pH 7.5, 50% loss of activity in 24 h, and complete loss of activity within one week
-
37C, 20 mM Tris-HCl, pH 7.5, 72% loss of activity in first two days
-
4C, 12 days, 57% residual activity
4C, 20 mM Tris-HCl, pH 7.5, 53% loss of activity in first two days. Addition of 25% glycerol preserves most of the activity
-
4C, 20 mM Tris-HCl, pH 7.5, stable for at least 20 days. Addition of 25% glycerol preserves most of the activity
-
4C, 80% saturated solution of ammonium sulfate, 10 days, 40% loss of activity
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
2 minor forms: AlaAT-1, AlaAT-3, 1 major form, AlaAT-2, ammonium sulfate, DEAE-cellulose, Sephacryl S-200, phenyl-Sepharose
-
ammonium sulfate, DEAE-cellulose, 3 isoforms
-
ammonium sulfate, DEAE-Sephadex, Sephadex G-200, partial purification
-
ammonium sulfate, DEAE-Sepharose, partial purification of cytosolic and mitochondrial isoenzymes
-
ammonium sulfate, hydroxylapatite, preparative electrophoresis
-
ammonium sulfate, Sephadex G-150, DEAE-Sephadex, partial purification
-
anaerobically induced isoform, ammonium sulfate, gel filtration, Q-Sepharose, Mono P, Mono Q
-
DEAE-Sephadex
-
Dowex 50WX8 200-400 mesh chromatography
-
heat treatment, ammonium sulfate, DEAE-cellulose, isoelectric focusing, Sephadex G-150, hydroxylapatite, DEAE-cellulose
-
heat treatment, ammonium sulfate, DEAE-Sepharose, hydroxylapatite, Sephacryl S-200
-
HisTrap HP column chromatography
-
native enzyme, Q-Sepharose, phenyl-Sepharose, hydroxyapatite, S-Sepharose, Mono Q, Superdex 200, recombinant enzyme, heat treatment, Mono Q
Ni2+-NTA agarose resin chromatography and Poly-Prep mini-column chromatography
-
recombinant enzyme
-
Sephadex G-150 column chromatography, DEAE-Sephadex A-25 column chromatography, and hydroxyapatite column chromatography
-
Sephadex G-150, DEAE-cellulose, ammonium sulfate, isoelectric focusing
-
Sepharose S12 gel filtration and nickel-chelating Sepharose column chromatography
using a DE52 column, butyl-Toyopearl column, DEAE-Toyopearl column, CHT ceramic hydroxyapatite column and MonoQ column
-
using anion exchange protein Pak Q 8HR column attached to HPLC system
-
using saline precipitation, gel filtration, preparative electrophoresis and anion exchange chromatography on protein-Pak Q 8HR column attached to HPLC
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Arabidopsis thaliana
-
expressed in Escherichia coli
-
expressed in Escherichia coli as a His-tagged fusion protein
expressed in Escherichia coli BL21 cells
-
expressed in Escherichia coli strain BL21gold(DE3)
-
expression as His-tagged protein
expression in Escherichia coli
expression in Sf9 cell
-
overexpressed as His6-tagged protein in Escherichia coli cells
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
ammonium as nitrogen source induces both gene expression and enzyme activity of AlaAT
-
ethanol administration causes a 3-3.5fold increase in serum ALT levels in superoxide dismutase deficient mice compared with their pair-fed controls and with wild-type ethanol-fed mice
-
hypoxia induces transcript levels for AlaAT1 but not AlaAT2. Hypoxia induces AlaAT1 earlier in roots than in shoots
-
in response to temperature changes, AlaAT levels reach a peak after 12 h in 10C water and after 48 h in 30Cwater, in response to salinity changes, AlaAT levels peak after 120 h in both 25 psu water (hyposalinity) and 45 psu water (hypersalinity)
-
nitrogen deprivation results in reduced transcript levels for AlaAT. The effect is more pronounced for AlaAT1
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
-
electrochemical immunosensor system for enzyme with detection limit of 10 pg/ml and 26.3 nA/(ng/ml), application as indicator for hepatocellular damage
additional information
-
a mutant strain is severely hampered in polyamine utilization, overview
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
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