Information on EC 2.6.1.36 - L-lysine 6-transaminase

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

EC NUMBER
COMMENTARY hide
2.6.1.36
-
RECOMMENDED NAME
GeneOntology No.
L-lysine 6-transaminase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
L-lysine + 2-oxoglutarate = (S)-2-amino-6-oxohexanoate + L-glutamate
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
amino group transfer
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
L-lysine degradation VI
-
-
Metabolic pathways
-
-
lysine metabolism
-
-
SYSTEMATIC NAME
IUBMB Comments
L-lysine:2-oxoglutarate 6-aminotransferase
A pyridoxal-phosphate protein. The product (L-allysine) is converted into the intramolecularly dehydrated form, (S)-2,3,4,5-tetrahydropyridine-2-carboxylate.
CAS REGISTRY NUMBER
COMMENTARY hide
9054-68-6
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Manually annotated by BRENDA team
Flavobacterium fuscum
-
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
5-N-acetyl-L-ornithine + 2-oxoglutarate
5-(N-acetylamino)-2-oxopentanoate + L-glutamate
show the reaction diagram
-
4.0% of the activity with L-lysine
-
-
?
6-N-acetyl-L-lysine + 2-oxoglutarate
6-(N-acetylamino)-2-oxohexanoate + L-glutamate
show the reaction diagram
-
5.7% of the activity with L-lysine
-
-
?
L-alanine + 2-oxoglutarate
pyruvate + L-glutamate
show the reaction diagram
-
very slow
-
-
?
L-lysine + 2-oxoadipate
2-aminoadipate 6-semialdehyde + L-homoglutarate
show the reaction diagram
-
7% of the activity with 2-oxoglutarate
-
-
?
L-lysine + 2-oxobutanoate
2-aminoadipate 6-semialdehyde + 2-aminobutanoate
show the reaction diagram
L-lysine + 2-oxoglutarate
(S)-2-amino-6-oxohexanoate + L-glutamate
show the reaction diagram
L-lysine + 2-oxoglutarate
2-aminoadipate 6-semialdehyde + 1-piperideine-6-carboxylic acid + L-glutamate
show the reaction diagram
-
product 2-aminoadipate 6-semialdehyde is further transformed to 1-piperideine-6-carboxylic acid, which may react with methylglyoxal to generate the acylated N-heterocyclic odorant 2-acetyltetrahydropyridine
-
?
L-lysine + 2-oxoglutarate
2-aminoadipate 6-semialdehyde + ?
show the reaction diagram
-
-
-
?
L-lysine + 2-oxoglutarate
2-aminoadipate 6-semialdehyde + L-glutamate
show the reaction diagram
L-lysine + 2-oxohexanoate
2-aminoadipate 6-semialdehyde + 2-aminohexanoate
show the reaction diagram
-
8.7% of the activity with 2-oxoglutarate
-
-
?
L-lysine + 2-oxopentanoate
2-aminoadipate 6-semialdehyde + 2-aminopentanoate
show the reaction diagram
L-lysine + oxaloacetate
2-aminoadipate 6-semialdehyde + L-aspartate
show the reaction diagram
L-lysine + pyruvate
2-aminoadipate 6-semialdehyde + L-alanine
show the reaction diagram
L-lysine hydroxamate + 2-oxoglutarate
? + L-glutamate
show the reaction diagram
-
5.1% of the activity with L-lysine
-
-
?
L-ornithine + 2-oxoglutarate
5-hydroxy-L-proline + glutamate
show the reaction diagram
L-ornithine + 2-oxoglutarate
? + L-glutamate
show the reaction diagram
L-thialysine + 2-oxoglutarate
? + L-glutamate
show the reaction diagram
-
13% of the activity with L-lysine
-
-
?
N-(2'-aminoethyl)-2,3-diaminopropionate + 2-oxoglutarate
2-aminoadipate 6-semialdehyde-hydroxamate + L-glutamate
show the reaction diagram
-
3.6% of the activity with L-lysine
-
-
?
N-alpha-benzyloxycarbonyl-L-ornithine + 2-oxoglutarate
N-benzyloxycarbonyl-5-hydroxy-L-proline + glutamate
show the reaction diagram
N-alpha-tert-butoxycarbonyl-L-ornithine + 2-oxoglutarate
N-tert-butoxycarbonyl-5-hydroxy-L-proline + glutamate
show the reaction diagram
S-(2-aminoethyl)-L-cysteine + 2-oxoglutarate
? + L-glutamate
show the reaction diagram
S-(2-N-acetylaminoethyl)-L-cysteine + 2-oxoglutarate
S-(2-N-acetylaminoethyl)-2-oxopropanoic acid + L-glutamate
show the reaction diagram
-
3.3% of the activity with L-lysine
-
-
?
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-lysine + 2-oxoglutarate
2-aminoadipate 6-semialdehyde + L-glutamate
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pyridoxal 5'-phosphate
pyridoxamine 5'-phosphate
-
can replace pyridoxal 5'-phosphate, Km: 0.00715 mM
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2,2'-oxybis[N'-[(E)-(4-fluorophenyl)methylidene]acetohydrazide]
-
25.6% cytotoxicity at 0.1 mM
2,2'-oxybis[N'-[(E)-[(3-benzyloxy)phenyl]methylidene]acetohydrazide]
-
26.4% cytotoxicity at 0.1 mM
2-oxopentanedioic acid
-
binding energy 6.48 kcal per mol
2-phenyl-4-(prop-2-yn-1-yloxy)-2,3-dihydro-1,3-thiazole-5-carboxylic acid
-
-
2-[methyl[(1-methylpiperidin-2-yl)methyl]amino]-1-phenylethanol
-
binding energy 7.23 kcal per mol
4-ethoxy-2-phenyl-2,3-dihydro-1,3-thiazole-5-carboxamide
-
protein is stabilzed in presence of the inhibitor
4-methoxy-2-(pyridin-4-yl)-2,3-dihydro-1,3-thiazole-5-carboxylic acid
-
at 0.05 mM, 24.87% cytotoxicity in a HEK-293 cell line
5-Aminopentanoate
-
-
5-hydroxylysine
-
DL-
acetate
-
stimulates alanine transamination, inhibits lysine transamination
Br-
-
stimulates alanine transamination, inhibits lysine transamination
Cl-
-
stimulates alanine transamination, inhibits lysine transamination
F-
-
stimulates alanine transamination, inhibits lysine transamination
formate
-
stimulates alanine transamination, inhibits lysine transamination
I-
-
stimulates alanine transamination, inhibits lysine transamination
N-([2-[2-(3,4-dimethoxyphenyl)ethyl]-1,3-dioxo-2,3,5,6,11,11a-hexahydro-1H-imidazo[1',5':1,6]pyrido[3,4-b]indol-5-yl]methyl)-2-(4-methoxyphenyl)acetamide
-
binding energy 10.79 kcal per mol
O-(2-aminoethyl)-DL serine
-
-
Phenylglyoxal
-
loss of activity with lysine, no effect on activity with L-alanine
propionate
-
inhibits alanine transamination and lysine transamination
additional information
-
incubation of the enzyme with L-lysine in the presence of high concentrations of phosphate gives an inactive form of the enzyme (semiapoenzyme), reactivation with pyridoxal 5'-phosphate
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
acetate
-
stimulates alanine transamination, inhibits lysine transamination
Br-
-
stimulates alanine transamination, inhibits lysine transamination
Cl-
-
stimulates alanine transamination, inhibits lysine transamination
F-
-
stimulates alanine transamination, inhibits lysine transamination
formate
-
stimulates alanine transamination, inhibits lysine transamination
I-
-
stimulates alanine transamination, inhibits lysine transamination
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.13 - 3.8
2-oxoglutarate
1.2 - 2.8
L-lysine
2
L-ornithine
-
pH 8.0, 37°C
2
S-(2-aminoethyl)-L-cysteine
-
pH 8.0, 37°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1 - 1.43
2-oxoglutarate
0.917 - 1.17
L-lysine
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00081
2,2'-oxybis[N'-[(E)-(4-fluorophenyl)methylidene]acetohydrazide]
Mycobacterium tuberculosis
-
pH not specified in the publication, temperature not specified in the publication
0.0019
2,2'-oxybis[N'-[(E)-[(3-benzyloxy)phenyl]methylidene]acetohydrazide]
Mycobacterium tuberculosis
-
pH not specified in the publication, temperature not specified in the publication
0.0018
2-phenyl-4-(prop-2-yn-1-yloxy)-2,3-dihydro-1,3-thiazole-5-carboxylic acid
Mycobacterium tuberculosis
-
pH 7.2, 37°C
0.0017
4-ethoxy-2-phenyl-2,3-dihydro-1,3-thiazole-5-carboxamide
Mycobacterium tuberculosis
-
pH 7.2, 37°C
0.0012
4-methoxy-2-(pyridin-4-yl)-2,3-dihydro-1,3-thiazole-5-carboxylic acid
Mycobacterium tuberculosis
-
pH 7.2, 37°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.12
pH 7.2, 37°C, wild-type enzyme
1.78
pH 7.2, 37°C, recombinant enzyme
18.67
-
pH 8.0, 37°C
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5
-
substrates L-ornithine + 2-oxoglutarate
8.3 - 8.5
-
substrates lysine + 2-oxoglutarate
9
-
substrate S-(2-aminoethyl)-L-cysteine
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 9.5
-
about 40% of maximum activity at pH 6 and pH 9.5, substrates ornithine + 2-oxoglutarate
7 - 10
-
pH 7: about 50% of maximum activity, pH 10: about 30% of maximum activity
7.2 - 10.2
-
about 50% of maximum activity at pH 7.2 and pH 10.2
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
PDB
SCOP
CATH
ORGANISM
UNIPROT
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
24000
-
1 * 24000 (A) + 1 * 28000 (B1) + 1 * 28000 (B2) + 1 * 45000-46000 (C), SDS-disc gel electrophoresis, gel filtration in presence of 6 M guanidine-HCl, equilibrium centrifugation in presence of 6 M urea
28000
-
1 * 24000 (A) + 1 * 28000 (B1) + 1 * 28000 (B2) + 1 * 45000-46000 (C), SDS-disc gel electrophoresis, gel filtration in presence of 6 M guanidine-HCl, equilibrium centrifugation in presence of 6 M urea
40000
-
2 * 40000, SDS-PAGE
48810
-
lysine epsilon-aminotransferase is a 450 amino acid protein
48900
x * 49890, calculated, x * 48900, SDS-PAGE
49890
calculated from sequence of cDNA; x * 49890, calculated, x * 48900, SDS-PAGE
51300
-
gel filtration
53000
-
2 * 53000, SDS-PAGE, 2 * 53300, deduced from gene sequence
53300
-
2 * 53000, SDS-PAGE, 2 * 53300, deduced from gene sequence
83000
-
gel filtration
110000
-
native PAGE
116000
-
sedimentation equilibrium method
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 49890, calculated, x * 48900, SDS-PAGE
tetramer
-
1 * 24000 (A) + 1 * 28000 (B1) + 1 * 28000 (B2) + 1 * 45000-46000 (C), SDS-disc gel electrophoresis, gel filtration in presence of 6 M guanidine-HCl, equilibrium centrifugation in presence of 6 M urea
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
docking experiments based on crystal structure PDB code 2CJH in order to identify enzyme inhibitors
-
hanging drop vapour diffusion method in 0.1 M trisodium citrate dihydrate solution containing 0.2 M ammonium acetate and 25% PEG 4000 in the pH range 5.4-6.0
-
molecular docking of inhibitors 4-methoxy-2-(pyridin-4-yl)-2,3-dihydro-1,3-thiazole-5-carboxylic acid, 2-phenyl-4-(prop-2-yn-1-yloxy)-2,3-dihydro-1,3-thiazole-5-carboxylic acid, 4-ethoxy-2-phenyl-2,3-dihydro-1,3-thiazole-5-carboxamide. Ligands are found in the vicinity of the Arg422, Gln274, Lys300, Arg170, Phe167, Glu243 amino acid residues. Compounds can make favourable interactions with important amino acid residues such as Arg170, Arg440, and Lys300
-
strcutures of mutants T330S, E243A, N328A, to 2.7-1.95 A resolution
-
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 7.5
-
55°C, 5 min, stable, partially purified enzyme
637017
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
50.6
-
melting temperature
52.1
-
melting temperature in presence of inhibitor 4-ethoxy-2-phenyl-2,3-dihydro-1,3-thiazole-5-carboxamide
55
-
pH 6.0-7.5, 5 min, stable, partially purified enzyme
65
-
5 min, activated by heat treatment
75
-
5 min, inactivation
additional information
-
pyridoxal 5'-phosphate, 0.1 mM, or 2-mercaptoethanol, 0.02%, protects against heat inactivation
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
pyridoxal 5'-phosphate, 0.1 mM, or 2-mercaptoethanol, 0.02%, protects against heat inactivation
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
0-5°C, crystalline enzyme, 0.2 M potassium phosphate buffer, pH 7.2, 50% saturation of ammonium sulfate, 0.1 mM pyridoxal 5'-phosphate, 0.01% 2-mercaptoethanol, stable for several weeks
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
lysine epsilon-aminotransferase is partially purified from a high-producing strain of Streptomyces lactamdurans
-
Ni2+-IDA column chromatography and Superdex S-200 gel filtration
-
partial
Sephacryl S-200 gel filtration
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21-DE3
-
expressed in Escherichia coli strain JM109; expression in Escherichia coli
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
in a hypoxia persistent model, enzyme expression is signifcantly upregulated
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E243A
-
mutation in acive-site residue. Mutant retains activity, but binds alpha-ketoglutarate in a different conformation
N328A
-
mutation in acive-site residue. Mutant binds pyridoxal 5'-phospate but is inactive
T330A
-
mutation in acive-site residue, mutant cannot bind pyridoxal 5'-phospate and is inactive
T330S
-
mutation in acive-site residue, mutant cannot bind pyridoxal 5'-phospate and is inactive
E243A
-
mutation in acive-site residue. Mutant retains activity, but binds alpha-ketoglutarate in a different conformation
-
N328A
-
mutation in acive-site residue. Mutant binds pyridoxal 5'-phospate but is inactive
-
T330A
-
mutation in acive-site residue, mutant cannot bind pyridoxal 5'-phospate and is inactive
-
T330S
-
mutation in acive-site residue, mutant cannot bind pyridoxal 5'-phospate and is inactive
-
additional information
-
fusion protein of enzyme to green fluorescent protein, study of temporal and spatial distribution of enzyme
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
biotechnology
-
production of beta-lactam antibiotics
nutrition
enzyme is involved in generation of mousy off-flavors in wine. Enzymic product 2-aminoadipate 6-semialdehyde is further transformed to 1-piperideine-6-carboxylic acid, which may react with methylglyoxal to generate the acylated N-heterocyclic odorant 2-acetyltetrahydropyridine
Show AA Sequence (241 entries)
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