Information on EC 1.4.1.13 - glutamate synthase (NADPH)

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

EC NUMBER
COMMENTARY hide
1.4.1.13
-
RECOMMENDED NAME
GeneOntology No.
glutamate synthase (NADPH)
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
2 L-glutamate + NADP+ = L-glutamine + 2-oxoglutarate + NADPH + H+
show the reaction diagram
L-glutamate + NADP+ + H2O = NH3 + 2-oxoglutarate + NADPH + H+
show the reaction diagram
1b
-
-
-
L-glutamate + NH3 = L-glutamine + H2O
show the reaction diagram
1a
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Alanine, aspartate and glutamate metabolism
-
-
Biosynthesis of antibiotics
-
-
Biosynthesis of secondary metabolites
-
-
L-glutamate biosynthesis I
-
-
L-glutamine degradation II
-
-
Metabolic pathways
-
-
Microbial metabolism in diverse environments
-
-
Nitrogen metabolism
-
-
glutamate and glutamine metabolism
-
-
SYSTEMATIC NAME
IUBMB Comments
L-glutamate:NADP+ oxidoreductase (transaminating)
Binds FMN, FAD, 2 [4Fe-4S] clusters and 1 [3Fe-4S] cluster. The reaction takes place in the opposite direction to that shown. The protein is composed of two subunits, alpha and beta. The alpha subunit is composed of two domains, one hydrolysing L-glutamine to NH3 and L-glutamate (cf. EC 3.5.1.2, glutaminase), the other combining the produced NH3 with 2-oxoglutarate to produce a second molecule of L-glutamate (cf. EC 1.4.1.4, glutamate dehydrogenase [NADP+]). The beta subunit transfers electrons to the cosubstrate. The NH3 is channeled through a 31 A channel in the active protein. In the absence of the beta subunit, coupling between the two domains of the alpha subunit is compromised and some ammonium can be produced. In the intact alphabeta complex, ammonia production only takes place as part of the overall reaction.
CAS REGISTRY NUMBER
COMMENTARY hide
37213-53-9
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
strain NCP262
Swissprot
Manually annotated by BRENDA team
strain NCP262
Swissprot
Manually annotated by BRENDA team
strain DSMZ 2266T
SwissProt
Manually annotated by BRENDA team
Methanococcus thermoautotrophicum
alpha-subunit
SwissProt
Manually annotated by BRENDA team
no activity in Arabidopsis thaliana
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
strain KOD1
-
-
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
phylogenetic and molecular evolutionary analyses; phylogenetic and molecular evolutionary analyses
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
L-glutamate + NADP+ + H2O
NH3 + 2-oxoglutarate + NADPH + H+
show the reaction diagram
-
-
-
?
L-glutamine + 2-oxoglutarate + NADPH
L-glutamate + NADP+
show the reaction diagram
L-glutamine + 2-oxoglutarate + NADPH + H+
L-glutamate + NADP+
show the reaction diagram
metronidazole + NADP+
? + NADPH
show the reaction diagram
NH3 + 2-oxoglutarate + NADPH + H+
L-glutamate + NADP+
show the reaction diagram
NH3 + 2-oxoglutarate + NADPH + H+
L-glutamate + NADP+ + H2O
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-glutamate + NADP+ + H2O
NH3 + 2-oxoglutarate + NADPH + H+
show the reaction diagram
A0A171, B3FYT6
-
-
-
?
L-glutamine + 2-oxoglutarate + NADPH
L-glutamate + NADP+
show the reaction diagram
NH3 + 2-oxoglutarate + NADPH + H+
L-glutamate + NADP+ + H2O
show the reaction diagram
A0A171, B3FYT6
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
flavin
additional information
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Fe2+
2[4Fe-4S]-containing enzyme; 2[4Fe-4S]-containing enzyme
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2',5'-ADP
-
act as a competitive ihibitor
2',5'-diphosphoadenylic acid
-
competitive inhibitor with respect to NADPH
2'-adenylic acid
2'-phosphoadenosine-5'-diphospho-5'-beta-D-ribose
2'-phosphoadenylic acid
-
competitive inhibitor with respect to NADPH
2,2'-bipyridyl
3-Aminopyridine adenine dinucleotide phosphate
3-Bromo-2-oxoglutarate
-
-
4-Iodoacetamidosalicylate
6-diazo-5-oxo-L-norleucine
acetyl-NADP+
-
-
AgNO3
-
at 0.001 mM completely inhibits
alpha-aminobutyrate
-
-
arginine
-
less than 45% inhibition
Atebrin
-
100% inhibition at 1 mM
azaserine
BaCl2
-
61% inhibition at 50 mM
Bromopyruvate
-
-
Butane-2,3-dione
-
slight inactivation
CaCl2
CdCl2
-
produces more than 60% inhibition at 5 mM
Cibacron blue 3GA
-
-
cis-aconitate
-
22% inhibition at 50 mM
citrate
-
slight
CoCl2
-
produces more than 60% inhibition at 5 mM
CTP
-
9% inhibition at 25 mM and 21% inhibition at 50 mM
D-glutamate
D-glutamine
-
-
D-Lysine
-
significantly inhibits
D-methionine
-
19% inhibition at 50 mM
dimethyl suberimidate
-
inactivates glutamine-dependent activity
DL-methionine DL-sulfoximine
DL-methionine sulfoxide
-
potent inhibitor
DL-Theanine
-
-
glycine
GTP
-
16% inhibition at 25 mM and 43% inhibition at 50 mM
HgCl2
-
at 0.001 mM remains 8% of activity
hydroxylamine
-
-
iodoacetamide
iodoacetate
iodonitrotetrazolium
-
inhibitor of the L-glutamate:iodonitrotetrazolim oxidoreductase activity of the alpha subunit at concentrations above 0.1 mM
isocitrate
ITP
-
17% inhibition at 25 mM and 29% inhibition at 50 mM
KCl
-
32% inhibition at 100 mM
KCN
-
89% inhibition at 20 mM
KNO3
-
47% inhibition at 100 mM
L-2-Amino-4-oxo-5-chloropentanoic acid
L-alanine
L-asparagine
L-aspartate
L-cysteine
-
significant inhibitor
L-fumarate
-
L-glutamate
L-histidine
L-homoserine
L-leucine
L-malate
L-methionine
L-methionine DL-sulfoximine
L-Methionine sulfone
L-MetS
-
reversible inhibitor
L-serine
L-tryptophan
-
strong inhibitor
lysine
methionine sulfone
-
-
MgCl2
MnCl2
N-ethylmaleimide
NAD+
-
competitive inhibition with NADH, noncompetitive inhibition with 2-oxoglutarate or L-glutamine
NADPH
NaN3
-
100% inhibition at 50 mM, 11% inhibition at 20 mM
NiCl2
-
produces more than 60% inhibition at 5 mM
O-carbamoylserine
-
competitive inhibitor vs. L-glutamine
o-phenanthroline
oxalate
-
48% inhibition at 5 mM
oxalglycine
-
-
oxaloacetate
oxalylglycine
-
competitive inhibitor vs. alpha-ketoglutarate, noncompetitive inhibitor vs. L-glutamine and uncompetitive vs. NADPH
p-chloromercuribenzoate
p-Chloromercuriphenylsulfonate
-
more than 50% loss in activity in 60 min at 0.05 mM
p-hydroxymercuribenzoate
-
complete inhibition at 1 mM, 5 min
phenylalanine
Phenylglyoxal
-
at 3 mM pyridoxal 5'-phosphate glutamine-dependent glutamate synthase is inactivated by about 50% within 10 min. This inactivation is not prevented by 2-oxoglutarate
putrescine
-
-
pyridoxal-5'-phosphate
-
52% inhibition of the glutamine-dependent reaction at 5 mM
pyruvate
Sodium arsenite
succinate
UTP
-
17% inhibition at 25 mM and 33% inhibition at 50 mM
valine
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
dimethyl suberimidate
-
increases NH3-dependent activity
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.009 - 2
2-oxoglutarate
0.017
acetylpyridine-NADPH
-
in the presence of 2.5 mM 2-oxo-glutarate and 5 mM L-glutamine, the apparent maximal velocity is 3.7% that obtained in the presence of NADPH
0.0047 - 0.35
alpha-ketoglutarate
0.14
ferricyanide
-
of NADPH: acceptor oxidoreductase activity of the beta subunit of the enzyme
0.05
iodonitrotetrazolium
-
of NADPH: acceptor oxidoreductase activity of the beta subunit of the enzyme
0.029 - 2.6
L-glutamine
0.035
menadione
-
of NADPH: acceptor oxidoreductase activity of the beta subunit of the enzyme
0.091 - 0.113
NADH
0.0022 - 16.3
NADPH
0.5 - 44
NH4Cl
0.01
thio-NADPH
-
in the presence of 2.5 mM 2-oxo-glutarate and 5 mM L-glutamine, the apparent maximal velocity is 54% that obtained in the presence of NADPH
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
39.5 - 41.9
ferricyanide
20 - 32
iodonitrotetrazolium
25.3
menadione
Azospirillum brasilense
-
of NADPH:acceptor oxidoreductase acitivity of the beta subunit of the enzyme
2.28 - 30.8
NADPH
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.106
2',5'-ADP
-
-
0.048
2',5'-diphosphoadenylic acid
-
-
2.1 - 17.2
2'-adenylic acid
0.0028
2'-phosphoadenosine 5'-diphospho-5-beta-D-ribose
-
-
0.021 - 0.495
2'-phosphoadenosine-5'-diphospho-5'-beta-D-ribose
0.0227 - 0.233
2'-phosphoadenosine-5'-diphosphoribose
0.186
2'-phosphoadenylic acid
-
-
0.0024 - 0.128
3-Aminopyridine adenine dinucleotide phosphate
0.0058
acetyl-NADP+
-
-
0.012
Cibacron blue 3GA
-
-
0.011 - 0.056
D-glutamate
0.02 - 0.76
DL-methionine DL-sulfoximine
25 - 45
glutamate
0.025
L-2-Amino-4-oxo-5-chloropentanoic acid
-
-
1.05
L-methionine
-
competitive inhibitor with respect to L-glutamine
0.022
L-methionine sulphone
-
-
-
0.48 - 5.5
methionine
0.01 - 0.045
methionine sulfone
0.02 - 1.13
NADP
0.0059 - 0.037
NADP+
0.8 - 20.6
oxalylglycine
0.86
p-chloromercuribenzoate
-
-
0.00023
thio-NADP+
-
-
additional information
additional information
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.24
-
apoenzyme lacking flavin and non-heme iron, glutamine-dependent activity
0.92
-
native enzyme, NH3-dependent activity
4.45
-
apoenzyme lacking flavin and non-heme iron, NH3-dependent activity
7.6
-
partially purified enzyme
14.3
-
native enzyme
18.64
-
native enzyme, glutamine-dependent activity
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5
-
optimum for both NH3-dependent and L-glutamine-dependent reaction
6.9
-
NADH-glutamine dependent activity
7.5 - 8.5
-
broad optimum
8.4
-
for glutamate synthesis, NH3-dependent glutamate synthase and apoenzyme
8.7
-
ammonia-dependent activity
9
-
ammonia-dependent activity
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.4 - 9
-
at pH 6.4 and 9.0 about 50% of activity maximum
6.5 - 8.7
-
at pH 6.5 and 8.7 about 50% of activity maximum
7.4 - 9.1
-
at pH 7.4 and 9.1 about 50% of activity maximum
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
75
-
glutamine-dependent reaction
80
-
glutamine-dependent reaction
90
-
NH3-dependent reaction
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
46000
x * 46000, deduced from gene sequence
50000
-
4 * 135000 + 4 * 50000, SDS-PAGE
51500
-
x * 175000 + x * 51500, SDS-PAGE
51900
x * 51900, pGLTY2, SDS-PAGE, x * 52000, pGLTY1, SDS-PAGE
52000
x * 51900, pGLTY2, SDS-PAGE, x * 52000, pGLTY1, SDS-PAGE
52400
x * 52400, SDS-PAGE
54000
-
1 * 158000 + 1 * 54000, SDS-PAGE
56000
-
1 * 160000 + 1 * 56000
72000
-
x * 72000 + x * 94000
94000
-
x * 72000 + x * 94000
135000
142000
-
x * 142000 + x * 55000, SDS-PAGE
145000
-
1 * 145000 + 1 * 55000, SDS-PAGE
152000
-
x * 152000 + x * 53000, SDS-PAGE
158000
-
1 * 158000 + 1 * 54000, SDS-PAGE
160000
175000
-
x * 175000 + x * 51500, SDS-PAGE
195000
-
sucrose density gradient centrifugation
200000
205000
-
gel filtration
210000
-
sucrose density sedimentation
220000
-
sucrose density gradient sedimentation
260000
-
gel filtration, in the absence of salt
280000
-
gel filtration
500000
-
gel filtration
740000
-
gel filtration
800000
840000
additional information
-
MW is salt-dependent
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
heterodimer
homodimer
2 * 200000, cryoelectron microscopy and small angle X-ray scattering
homohexamer
6 * 200000, cryoelectron microscopy and small angle X-ray scattering, the hexamer exhibits a concentration-dependent equilibrium with monomers and dimers, in solution the hexamer is destabilized by high ionic strength and to a lower extent by the reaction product NADP+
octamer
tetramer
additional information
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.3 - 8.3
-
-
391446
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
-20
-
complete loss of activity after 10 days
-10
-
stable for at least 6 weeks
0
-
stable for 6-8 h in crude extract
4
-
unprotected enzyme loses 90% of activity in 48 hours, protected enzyme, addition of 5 mM EDTA and 5 mM 2-mercaptoethanol or 1 mM DTT retains 80 to 90% of the activity after 48 hours
40
-
10 min, 80% loss of activity, enzyme in crude extract
55
-
10 min, in 0.1 M potassium phosphate buffer, pH 6.8, 70-80% loss of activity
70 - 100
purified enzyme, 10 min, stable up to 90°C; purified enzyme, 10 min, stable up to 90°C
80
-
10 min, 35% loss of activity
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
2 mM alpha-ketoglutarate, 10 mM beta-mercaptoethanol and 10% glycerol when present together markedly enhance stability
-
2-mercaptoethanol, stabilizes
alpha-ketoglutarate stabilizes
alpha-ketoglutarate, L-glutamine, L-glutamate and NADP when present together partial protect against enzyme inactivation
-
DTT, 1 mM, stabilizes at 4°C
-
EDTA, stabilizes
glutamine stabilizes
incubation with L-glutamine or L-glutamate results in marked time- and temperature-dependent loss in activity
-
NADP causes relatively small loss in activity compared with control values
-
unprotected enzyme is unstable, losing 65% of its activity in 24 hours at 4°C
-
OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
presence of reducing agents is essential for stabilization
-
391440
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-80°C, 20 mM potassium-HEPES, pH 7.2, 2 mM alpha-ketoglutarate, 1 mM EDTA, stable for at least 6 months
-
4°C, 20 mM potassium-HEPES, pH 7.2, 2 mM alpha-ketoglutarate, 1 mM EDTA, 5 mM 2-mercaptoethanol, 20% loss of activity, after 1 month
-
4°C, 200 mM potassium phosphate buffer, pH 7.6, 0.5 mM Na2EDTA
-
4°C, unprotected enzyme loses 65% of activity after 24 h
-
storing at -20°C, total loss of activity after 10 days
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
of the alpha subunit, using column chromatography on Q-Sepharose and Ultrogel AcA34
-
of the G298A-beta subunit, using column chromatography on Reactive Red or Amicon Red resins and gel filtration on Ultrogel AcA 34
-
of the recombinant enzyme beta subunit, using ammonium sulfate fractionation, affinity chromatography on Reactive Red, ultrafiltration and column chromatography on Ultrogel AcA 54
-
of the recombinant enzyme from overproducing Escherichia coli cells, using ion exchange chromatography on Q-Sepharose, gel filtration on Sephacryl S-300 and affinity chromatography on 2',5' ADP-Sepharose 4B colum
-
partial purification using column chromatography on DEAE-cellulose
-
partial, using ultrasonic oscillation, ammonium sulfate precipitation, column chromatography on Sephacryl S300 and DE-52 cellulose
-
recombuinant enzyme and isolated beta subunit
-
using ammonium sulfate fractionation, column chromatography on DEAE-cellulose and Blue-Sepharose
-
using ammonium sulfate fractionation, column chromatography on DEAE-cellulose and Sephadex G-200
-
using ammonium sulfate fractionation, column chromatography on DEAE-cellulose, Sepharose 6B, hydroxyapatite, glutamate dehydrogenase antibody affinity chromatography and column chromatography on Sephacryl S-200
-
using ammonium sulfate fractionation, coulmn chromatography on DEAE-cellulose, hydroxyapatite, Sepharose 6B and Sephadex G-200
-
using ammonium sulfate fractionation, gel filtration on Sephacryl S-300 and affinity chromatography on NADPH-Sepharose
-
using ammonium sulfate precipitation and column chromatography on DEAE-Sepharose, 2',5'-ADP-Sepharose and Sephacryl S-300
-
using heat treatment, ammonium sulfate precipitation, column chromatography on DEAE-Trisacryl, gel filtration and affinity chromatogray
-
using heat treatment, anion-exchange column chromatography on HiTrap Q and cation exchange column chromatography on Resources S
-
using protamine sulfate precipitation, ammonium sulfate precipitation, column chromatography on DE52, DEAE-Sephadex, hydroxyapatite, phenyl-Sepharose CL-4B and Bio-Gel filtration
-
using sonication, heat treatment, protamine sulfate precipitation, ammonium sulfate precipitation, gel filtration on G-50, column chromatography on DEAE-Sephadex and gel filtration on Sephadex G-200 and Sepharose 6B
-
using streptomycin sulfate treatment, ammonium sulfate fractionation, heat treatment, agarose gel filtration and DEAE-cellulose column chromatography
-
using streptomycin sulfate treatment, ammonium sulfate precipitation, column chromatography on DEAE-Sephacel, Bio-Gel A 1.5 m, Red Sepharose CL6B and Sephadex G-25
-
using streptomycin sulfate treatment, ammonium sulfate precipitation, column chromatography on Ultrogel AcA 22 and DEAE-Sephadex A-50, ultrafiltration with an Amicon PM 30 membrane and chromatography on hydroxyapatite column
-
using sulfate precipitation, gel filtration and column chromatography on 2',5'-ADP-Sepharose
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination and analysis, sequence comparison, quantitative real-time PCR expression analysis, recombinant expression in Escherichia coli strain BL21(DE3); DNA and amino acid sequence determination and analysis, sequence comparison, quantitative real-time PCR expression analysis, recombinant expression in Escherichia coli strain BL21(DE3)
expressed in Escherichia coli BL21 (DE3) cells
expression in GOGAT large subunit-deficient Escherichia coli JRG72 mutants
expression of the holoenzyme in Escherichia coli
-
gene PH0876, DNA and amino acid sequence determination and analysis, phylogenetic analysis, expression in Escherichia coli strain Rosetta (DE3); gene PH1873, DNA and amino acid sequence determination and analysis, phylogenetic analysis, expression in Escherichia coli strain Rosetta (DE3)
overproduction of the holoenzyme and of the alpha subunit in Escherichia coli
-
production of the alpha and beta subunits in Escherichia coli
-
production of the beta subunit in Escherichia coli
-
production of the G298A-beta subunit in Escherichia coli
-
the gltA gene encoding the enzyme overexpressed in Escherichia coli
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C47A
-
beta subunit, no significant effect on NADPH:iodonitrotetrazolium oxidoreductase activity of subunit, complete loss of activity of enzyme
C50A
-
beta subunit, no significant effect on NADPH:iodonitrotetrazolium oxidoreductase activity of subunit, complete loss of activity of enzyme
C55A
-
beta subunit, no significant effect on NADPH:iodonitrotetrazolium oxidoreductase activity of subunit, complete loss of activity of enzyme
C59A
-
beta subunit, no significant effect on NADPH:iodonitrotetrazolium oxidoreductase activity of subunit, complete loss of activity of enzyme
G298A
-
mutant with an approximately 10fold decrease of the affinity of the enzyme for pyridine nucleotides with little or no effect on the rate of the enzyme reduction by NADPH, maintains the ability to bind NADPH and FAD, is catalytically active in the NADPH:iodonitrotetrazolium oxidoreductase reaction and has a monomeric state, mutation leads to production of insoluble protein under conditions that yield large amounts of soluble wild-type enzyme and to production of smaller amounts of enzyme
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
molecular biology
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