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Information on EC 5.4.3.3 - lysine 5,6-aminomutase and Organism(s) Acetoanaerobium sticklandii and UniProt Accession E3PRJ5
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5.4.3.3 lysine 5,6-aminomutaseIUBMB Comments
This enzyme is a member of the 'AdoMet radical' (radical SAM) family. It requires pyridoxal 5'-phosphate and adenosylcobalamin for activity. A 5'-deoxyadenosyl radical is generated during the reaction cycle by reductive cleavage of adenosylcobalamin, which is regenerated at the end of the reaction.
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Word Map
- 5.4.3.3
- adenosylcobalamin
- pyridoxal-5'-phosphate
-
paramagnetic
- sticklandii
- pyridoxal
-
cobiialamin
-
adenosylcobalamin-dependent
-
homolysis
-
5\'-deoxyadenosyl
- 5'-phosphate
-
4,5-aminomutase
-
5\'-deoxyadenosylcobalamin
-
aldimine
- l-beta-lysine
- d-ornithine
-
pyridoxal-5'-phosphate-dependent
-
substrate-related
- dl-lysine
-
1,2-amino
-
cobalamin-dependent
-
adocbl
-
plp-binding
-
adenosyl
- 5'-deoxyadenosine
-
plp-dependent
-
transaldimination
-
spin-coupled
-
cobalamin-binding
-
hyperfine
The taxonomic range for the selected organisms is: Acetoanaerobium sticklandii
The expected taxonomic range for this enzyme is: Bacteria, Archaea
The expected taxonomic range for this enzyme is: Bacteria, Archaea
Reaction Schemes
Synonyms
lysine 5,6-aminomutase, 5,6-lam, kamde, d-lysine 5,6-aminomutase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
5,6-LAM
lysine 5,6-aminomutase
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
(3S)-3,6-diaminohexanoate = (3S,5S)-3,5-diaminohexanoate
steric course and mechanistic aspects
-
(3S)-3,6-diaminohexanoate = (3S,5S)-3,5-diaminohexanoate
catalytic mechanism, overview
-
(3S)-3,6-diaminohexanoate = (3S,5S)-3,5-diaminohexanoate
reaction mechanism, detailed overview
(3S)-3,6-diaminohexanoate = (3S,5S)-3,5-diaminohexanoate
catalytic mechanism, the closed-state of the enzyme is required to bring the cofactors adenosylcobalamin and pyridoxal 5'-phosphate and the substrate into proximity for the radical-mediated 1,2-amino group migration. This process is achieved by transaldimination of the pyridoxal 5'-phosphate-Lys144beta internal aldimine with the pyridoxal 5'-phosphate-substrate external aldimine
-
(3S)-3,6-diaminohexanoate = (3S,5S)-3,5-diaminohexanoate
radical catalytic mechanism
-
(3S)-3,6-diaminohexanoate = (3S,5S)-3,5-diaminohexanoate
radical stabilization is crucial in the mechanism of action of lysine 5,6-aminomutase, role of Tyr263alpha. The enzyme utilizes free radical intermediates to mediate 1,2-amino group rearrangement, during which an elusive high-energy aziridincarbinyl radical is proposed to be central in the mechanism of action. The aziridincarbinyl radical acts either as a spin-relay device or serves as an anchor for the pyridine ring of pyridoxal-5' -phosphate through aromatic PI-stacking interactions during spin transfer, detailed overview
-
(3S)-3,6-diaminohexanoate = (3S,5S)-3,5-diaminohexanoate
in the first step of the proposed catalytic cycle the enzyme accepts the substrate in the open state. Substrate interactions with the active site residues initiate an external aldimine formation with PLP breaking the pyridoxal 5'-phosphate-lys144beta internal aldimine, which results in two simultaneous events: (1) the domain motion brings dAdoCbl close to the pyridoxal 5'-phosphate-substrate adduct and locks the enzyme in the catalytically active closed state and (2) cleavage of the Co-C bond of dAdoCbl generates the 5'-deoxyadenosyl radical and cob(II)alamin. Hydrogen abstraction by 5'-deoxyadenosyl radical from the substrate generates deoxyadenosine and the substrate related radical that undergoes radical isomerization via a hypothetical azacyclopropylcarbinyl radical to afford the product related radical. Hydrogen abstraction by the product related radical from deoxyadenosine generates the product-pyridoxal 5'-phosphate adduct and 5'-deoxyadenosyl radical. Finally, transition from the closed state to open state occurs, which allows the release of the product and reformation of dAdoCbl and the internal aldimine
D-lysine = (2R,5S)-2,5-diaminohexanoate
catalytic mechanism, overview
-
D-lysine = (2R,5S)-2,5-diaminohexanoate
catalytic mechanism, the closed-state of the enzyme is required to bring the cofactors adenosylcobalamin and pyridoxal 5'-phosphate and the substrate into proximity for the radical-mediated 1,2-amino group migration. This process is achieved by transaldimination of the pyridoxal 5'-phosphate-Lys144beta internal aldimine with the pyridoxal 5'-phosphate-substrate external aldimine
-
D-lysine = (2R,5S)-2,5-diaminohexanoate
radical stabilization is crucial in the mechanism of action of lysine 5,6-aminomutase, role of Tyr263alpha. The enzyme utilizes free radical intermediates to mediate 1,2-amino group rearrangement, during which an elusive high-energy aziridincarbinyl radical is proposed to be central in the mechanism of action. The aziridincarbinyl radical acts either as a spin-relay device or serves as an anchor for the pyridine ring of pyridoxal-5' -phosphate through aromatic PI-stacking interactions during spin transfer, detailed overview
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
isomerization
isomerization
-
-
-
-
PATHWAY SOURCE
PATHWAYS
BRENDA
-
-
SYSTEMATIC NAME
IUBMB Comments
(3S)-3,6-diaminohexanoate 5,6-aminomutase
This enzyme is a member of the 'AdoMet radical' (radical SAM) family. It requires pyridoxal 5'-phosphate and adenosylcobalamin for activity. A 5'-deoxyadenosyl radical is generated during the reaction cycle by reductive cleavage of adenosylcobalamin, which is regenerated at the end of the reaction.
CAS REGISTRY NUMBER
COMMENTARY
9075-69-8
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
4-thia-(R)-lysine
?
-
4-thia-(R)-lysine reacts with the complex of pyridoxal 5'-phosphate, adenosylcobalamin, and lysine 5,6-aminomutase to generate cob(II)alamin, 5'-deoxyadenosine, and 4-thialysine-based free radicals
-
-
?
4-thia-(S)-lysine
?
-
4-thia-(S)-lysine reacts with the complex of pyridoxal 5'-phosphate, adenosylcobalamin, and lysine 5,6-aminomutase to generate cob(II)alamin, 5'-deoxyadenosine, and 4-thialysine-based free radicals
-
-
?
(3S)-3,6-diaminohexanoate
(3S,5S)-3,5-diaminohexanoate
-
-
-
-
r
(3S)-3,6-diaminohexanoate
(3S,5S)-3,5-diaminohexanoate
-
-
-
r
3,6-Diaminohexanoate
3,5-Diaminohexanoate
-
-
(3S,5S)-3,5-diaminohexanoate
?
3,6-Diaminohexanoate
3,5-Diaminohexanoate
-
(3S)-beta-lysine
(3S,5S)-3,5-diaminohexanoate
?
L-lysine
2,5-diaminohexanoate
-
first step in D-lysine catabolism
-
r
additional information
?
-
-
5-fluorolysine as substrate binding in the active site: computational simulations, the enzyme 5,6-LAM abstracts the hydrogen atom rather than the fluorine at C5 of 5-fluorolysine and subsequent rearrangement mimicking the similar mechanism as the natural substrate of the enzyme
-
-
?
additional information
?
-
-
the enzyme can accept D-lysine and L-beta-lysine
-
-
?
additional information
?
-
-
the enzyme can accept D-lysine and L-beta-lysine
-
-
?
additional information
?
-
-
the enzyme can accept D-lysine and L-beta-lysine. The enzyme employs radical generating capability of coenzyme B12, i.e. 5'-deoxyadenosylcobalamin, and ability of pyridoxal 5'-phosphate, i.e. vitamin B6, to stabilize high-energy intermediates for performing challenging 1,2-amino rearrangements between adjacent carbons
-
-
?
additional information
?
-
-
the enzyme can accept D-lysine, L-lysine, and L-beta-lysine. The enzyme employs radical generating capability of coenzyme B12, i.e. 5'-deoxyadenosylcobalamin, and ability of pyridoxal-5'-phosphate, i.e.vitamin B6, to stabilize high-energy intermediates for performing challenging 1,2-amino rearrangements between adjacent carbons
-
-
?
additional information
?
-
lysine 5,6-aminomutase, 5,6-LAM, catalyzes the reversible amino shift between C6 and C5 of D-lysine and L-beta-lysine. 5,6-LAM is a 5'-deoxyadenosylcobalamin and pyridoxal 5'-phosphate co-dependent radical enzyme, molecular mechanism of the open-closed protein conformational cycle transitions and coupled substrate binding, activation and product release events in lysine 5,6-aminomutase, overview
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
L-lysine
2,5-diaminohexanoate
-
first step in D-lysine catabolism
-
r
(3S)-3,6-diaminohexanoate
(3S,5S)-3,5-diaminohexanoate
-
-
-
-
r
(3S)-3,6-diaminohexanoate
(3S,5S)-3,5-diaminohexanoate
-
-
-
r
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
5'-deoxyadenosylcobalamin
-
shows ability to produce highly reactive 5'-deoxyadenosyl radical in enzymatic environments, situated in the Rossmann domain in the crystal structure, and separated from pyridoxal 5'-phosphate
5'-deoxyadenosylcobalamin
-
shows ability to produce highly reactive 5'-deoxyadenosyl radical in enzymatic environments, situated in the Rossmann domain in the crystal structure, and separated from pyridoxal-5'-phosphate
adenosylcobalamin
-
Km value 6.1 mM, in presence of S-subunit of D-ornithine aminomutase, Km value 3.5 mM, in presence of ATP and S-subunit of D-ornithine aminomutase, Km value 1.9 mM
Cobalamin
-
required, directly involved in the catalysis of the amino group migration
Cobalamin
-
coenzyme serves as carrier of the hydrogen that is transferred
pyridoxal 5'-phosphate
-
Km value 3.9 mM, in presence of S-subunit of D-ornithine aminomutase, Km value 3.0 mM, in presence of ATP and S-subunit of D-ornithine aminomutase, Km value 2.4 mM
pyridoxal 5'-phosphate
-
dependent on, molecular modeling in the reaction
pyridoxal 5'-phosphate
-
stabilizes high-energy intermediates for performing challenging 1,2-amino rearrangements between adjacent carbons, bound at the top of the TIM barrel domain and separated from 5'-deoxyadenosylcobalamin, binding site structure involving residues Tyr263, Asn299, Arg184, Arg268, Ser189, Gly187, Gln188, and Ser189, overview
additional information
-
the closed-state of the enzyme is required to bring the cofactors adenosylcobalamin and pyridoxal 5'-phosphate and the substrate into proximity for the radical-mediated 1,2-amino group migration. This process is achieved by transaldimination of the pyridoxal 5'-phosphate-Lys144beta internal aldimine with the pyridoxal 5'-phosphate-substrate external aldimine
-
additional information
lysine 5,6-aminomutase is a 5'-deoxyadenosylcobalamin and pyridoxal 5'-phosphate co-dependent radical enzyme
-
additional information
lysine 5,6-aminomutase is a 5'-deoxyadenosylcobalamin and pyridoxal 5'-phosphate co-dependent radical enzyme, formation of internal aldimine with pyridoxal 5'-phosphate and pyridoxal 5'-phosphate-N-oxide
-
additional information
lysine 5,6-aminomutase shows flexibility toward cofactor analogue pyridoxal 5'-phosphate-N-oxide, which can act as a functional cofactor for enzyme 5,6-LAM, kinetics and structure-function analysis, overview
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
K+
Mg2+
Rb+
Zn2+
-
purified KamDE contains a substantial quantity of metal ions, primarily Zn2+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Hydroxyadenylcobamide
-
formed during isolation by degradation of enzyme-bound cobamide, strong inhibitor, tightly bound to the protein. Incubation with cobalamin, Mg2+, a mercaptan, and pyridoxal 5'-phosphate displaces the hydroxyadenylcobamide and markedly activates the enzyme
iodoacetamide
-
cobamide enzyme compound is unaffected, sulfhydryl enzyme compounds is rapidly inactivated
additional information
-
during catalysis under conditions where the mutase product 3,5-diaminohexanoate is not continuously removed there is extensive cleavage of cobamamide coenzyme to free 5'-deoxyadenosine and cobalamin with concomitant inactivation of the enzyme. This inactivation is prevented by the addition of sulfhydryl protein and ATP, oxygen accelerates inactivation
-
additional information
-
homologues of substrate D-lysine, D-2,5-diaminopentanoic acid, 2,4-diaminobutyric acid, and D-2,3-diaminopropionic acid bind to pyridoxal 5'-phosphate as an external aldimine and elicit the 5'-deoxyadenosylcobalamin Co-C bond homolysis and the accumulations of cob(II)alamin and analogue-based radicals. The position for hydrogen atom abstraction from D-2,5-diaminopentanoic acid and 2,4-diaminobutyric acid by the 5'-deoxyadenosyl radical occurs at the carbon adjacent to the imine, resulting in overstabilized radicals by spin delocalization through the imine into the pyridine ring of pyridoxal 5'-phosphate. These radicals block the active site, inhibit the enzyme, and poise the enzyme into two distinct conformations: for even-numbered analogues, the cob(II)alamin remains proximal to and spin-coupled with the analogue-based radical in the closed state while odd-numbered analogues trigger the transition to the open state of the enzyme, inactivation mechanism, overview
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2-oxobutanoate
-
can partially replace pyruvate, which is required for reaction
additional information
-
presence of enzyme component E2 in the assay mixture induces ATP to activate enzyme component E1 allosterically
-
ATP
-
protein KamDE comprised of the 30000 and 51000 Da subunits of the E1 component of D-alpha-lysine aminomutase is catalytically active in absence of the third 128000 Da subunit, but ATP no longer has a regulatory effect on it. The S subunit of D-ornithine aminomutase, OraS, is capable of forming a complex with KamDE and restores the enzymes ATP-dependent allosteric regulation. ATP lowers the Km value of the KamDE-OraS complex for adenosylcobalamin and pyridoxal phosphate
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
20
(3R)-3,6-diaminohexanoate
-
pH and temperature not specified in the publication
8.7
(3S)-3,6-diaminohexanoate
-
pH and temperature not specified in the publication
additional information
additional information
kinetic parameters of enzyme 5,6-LAM are measured using D-lysine or isotope-labeled D-lysine-4,4,5,5-d4 as a substrate, overview
-
0.02
D-Lysine
-
pH and temperature not specified in the publication
1
D-Lysine
with pyridoxal 5'-phosphate N-oxide as cofactor, pH 8.5, 37°C
14.2
D-Lysine
with pyridoxal 5'-phosphate as cofactor, pH 8.5, 37°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1
D-Lysine
with pyridoxal 5'-phosphate N-oxide as cofactor, pH 8.5, 37°C
14.2
D-Lysine
with pyridoxal 5'-phosphate as cofactor, pH 8.5, 37°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0004
(3R)-3,6-diaminohexanoate
-
pH and temperature not specified in the publication
0.48
(3S)-3,6-diaminohexanoate
-
pH and temperature not specified in the publication
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
19.5
-
unit defined as the amounts which allows the formation of 0.001 mM NADPH per min in a coupled assay system
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
8.5
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
8 - 10.5
-
pH 8.0: about 55% of maximal activity, pH 10.5: about 65% of maximal activity, no activity at pH 7
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
-
the enzyme belongs to the class III dAdoCbl-dependent isomerase family
malfunction
the D298N, D298A, K370Q, and K370A variants of the alpha-subunits abolish the enzymatic activity in converting D-lysine into D-2,5-diaminohexanoic acid
metabolism
additional information
metabolism
-
lysine 5,6-aminomutase is essential for the metabolism of L- or D-lysine in anaerobic bacteria
metabolism
-
the enzyme participates in the second step of the fermentation pathway of lysine in which lysine is converted to acetic acid, ammonia and butyric acid
additional information
-
active site structure, overview. A large-scale domain movement is required for interconversion between the catalytically inactive open form and the catalytically active closed form. The recombinant enzyme (KamDE) containing only E1 is active, but is subjected to suicide inactivation with the substrate. Modeling of the closed conformation of the enzyme, domain motions, overview
additional information
-
the closed-state of the enzyme is required to bring the cofactors adenosylcobalamin and pyridoxal 5'-phosphate and the substrate into proximity for the radical-mediated 1,2-amino group migration. This process is achieved by transaldimination of the pyridoxal 5'-phosphate-Lys144beta internal aldimine with the pyridoxal 5'-phosphate-substrate external aldimine
additional information
both Asp298alpha and Lys370alpha are functionally important residues in enzyme 5,6-LAM
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
29191
-
alpha2,beta2, 2 * 57261 + 2 * 29191, deduced from nucleotide sequence
300000
-
2 * 55000, alpha-subunit + 2 * 300000, beta-subunit, alpha2beta2
55000
57261
-
alpha2,beta2, 2 * 57261 + 2 * 29191, deduced from nucleotide sequence
60000
-
x * 60000, gel filtration, sulfhydryl component, x * about approximately 150000, gel filtration, cobamide protein component
55000
-
2 * 55000, alpha-subunit + 2 * 300000, beta-subunit, alpha2beta2
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
-
x * 60000, gel filtration, sulfhydryl component, x * about approximately 150000, gel filtration, cobamide protein component
heterotetramer
alpha2beta2, subunits alpha and beta are encoded by genes kamD and kamE
tetramer
additional information
tetramer
-
alpha2,beta2, 2 * 57261 + 2 * 29191, deduced from nucleotide sequence
tetramer
-
2 * 55000, alpha-subunit + 2 * 300000, beta-subunit, alpha2beta2
additional information
-
protein KamDE comprised of the 30 and 51 kDa subunits of the E1 component of D-alpha-lysine aminomutase is catalytically active in absence of the third 12.8 kDa subunit, but ATP no longer has a regulatory effect on it. The S subunit of D-ornithine aminomutase, OraS, is capable of forming a complex with KamDE and restores the enzymes ATP-dependent allosteric regulation
additional information
-
the enzyme comprises two protein components, the core enzyme E1 and an auxiliary activating protein E2. E1 is a 170 kDa heterotetramer composed of 55 kDa alpha-subunits and 30 kDa beta-subunits and formulated as alpha2beta2, whereas the molecular mass of E2 is about 80 kDa. E2 shows dAdoCbl synthetase activity when isolated separately. A large-scale domain movement is required for interconversion between the catalytically inactive open form and the catalytically active closed form
additional information
the beta-Rossmann subunit binds dAdoCbl in a base-off mode with the axial 5,6-dimethylbenzimidazole ligand displaced by His133beta. The alpha-triosephosphate isomerase barrel binds pyridoxal 5'-phosphate, which is also covalently bound as a Schiff base (internal aldimine) to Lys144beta, forming a cross-link between the subunits. The distance between dAdoCbl and pyridoxal 5'-phosphate is 24 A. This configuration represents the open state of the enzyme
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging-drop vapor diffusion method, X-ray structure of substrate-free form, space group P3(1)2(1) with one alphabeta heterodimer per asymmetric unit, a = b = 99.7 A, c = 168.8 A, 2.8 A resolution
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D298A
site-directed mutagenesis, the mutation of the alpha-subunit
D298N
site-directed mutagenesis, the mutation of the alpha-subunit reduces the enzymatic activity in converting D-lysine into D-2,5-diaminohexanoic acid
K370A
site-directed mutagenesis, the mutation of the alpha-subunit reduces the enzymatic activity in converting D-lysine into D-2,5-diaminohexanoic acid
K370Q
site-directed mutagenesis, the mutation of the alpha-subunit reduces the enzymatic activity in converting D-lysine into D-2,5-diaminohexanoic acid
additional information
-
protein KamDE comprised of the 30000 and 51000 kDa subunits of the E1 component of D-alpha-lysine aminomutase is catalytically active in absence of the third 12800 kDa subunit, but ATP no longer has a regulatory effect on it. The S subunit of D-ornithine aminomutase, OraS, is capable of forming a complex with KamDE and restores the enzymes ATP-dependent allosteric regulation. OraS protein alone lowers the Km of KamDE for adenosylcobalamin and pyridoxal phosphate
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
35 - 55
-
approx. 50% loss of activity at 43°C after 5 min, almost complete loss of activity at 55°C after 5 min
70
-
10 min, sulfhydryl component is destroyed, cobamide protein component loses about 40% of its activity
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
highly purified sulfhydryl-enzyme-component is relatively unstable in dilute solutions of low ionic strength. The presence of mercaptans in buffers tends to prevent aggregation. The cobamide enzyme component is stable to a variety of storage conditions even when highly purified
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-15°C, Tris buffer, pH 8.5-9.0, protein concentration of no less than 3 mg/ml, 20-40% loss of activity after 1 month
-
-18°C, partially purified enzyme in solutions containing phosphate or ammonium sulfate
-
-20°C, 50% glycerol, protein KamDE comprised of the 30000 and 51000 Da subunits of the E1 component of D-alpha-lysine aminomutase can be stored for several months with significant loss of activity
-
-22°C, stable for at least 3 months. After 6 months, with repeated freezing and thawing, two-third of the original activity remains
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
protein KamDE comprised of the 30000 and 51000 Da subunits of the E1 component of D-alpha-lysine aminomutase, expression in Escherichia coli
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
genes kamD and kam E encode subunits alpha and beta
genes kamDE coding for the 30000 and 51000 Da subunits of the E1 component of D-alpha-lysine aminomutase, expression in Escherichia coli
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Stadtman, T.C.; Renz, P.
Anaerobic degradation of lysine. V. Some properties of the cobamide coenzyme-dependent beta-lysine mutase of Clostridium sticklandii
Arch. Biochem. Biophys.
125
226-239
1968
Acetoanaerobium sticklandii
Stadtman, T.C.; Grant, M.A.
L-beta-Lysine mutase (Clostridium sticklandii)
Methods Enzymol.
17B
206-211
1971
Acetoanaerobium sticklandii
-
Baker, J.J.; van der Drift, C.; Stadtman, T.C.
Purification and properties of beta-lysine mutase, a pyridoxal phosphate and B12 coenzyme dependent enzyme
Biochemistry
12
1054-1063
1973
Acetoanaerobium sticklandii
Kunz, F.; Retey, J.; Arigoni, D.; Tsai, L.; Stadtman, T.C.
Die absolute Konfiguration der 3,5-Diaminohexansure aus der beta-Lysin-Mutase-Reaktion
Helv. Chim. Acta
61
1139-1145
1978
Acetoanaerobium sticklandii
-
Retey, J.; Kunz, F.; Arigoni, D.; Stadtman, T.C.
Zur Kenntnis der beta-Lysin-Mutase-Reaktion: Mechanismus und sterischer Verlauf
Helv. Chim. Acta
61
2989-2998
1978
Acetoanaerobium sticklandii
-
Stadtman, T.C.; Tsai, L.
A cobamide coenzyme dependent migration of the e-amino group of D-lysine
Biochem. Biophys. Res. Commun.
28
920-926
1967
Acetoanaerobium sticklandii
Morley, C.G.D.; Stadtman, T.C.
Studies on the fermentation of D-alpha-lysine. Purification and properties of an adenosine triphosphate regulated B12-coenzyme-dependent D-alpha-lysine mutase complex from Clostridium sticklandii
Biochemistry
9
4890-4900
1970
Acetoanaerobium sticklandii
Morley, C.G.D.; Stadtman, T.C.
The role of pyridoxal phosphate in the B12-coenzyme-dependent D-alpha-lysine mutase reaction
Biochemistry
11
600-605
1972
Acetoanaerobium sticklandii
Morley, C.G.D.; Stadtman, T.C.
Studies on the fermentation of D-alpha-lysine. On the hydrogen shift catalyzed by the B12 coenzyme dependent D-alpha-lysine mutase
Biochemistry
10
2325-2329
1971
Acetoanaerobium sticklandii
Chang, C.H.; Frey, P.A.
Cloning, sequencing, heterologous expression, purification, and characterization of adenosylcobalamin-dependent D-lysine 5, 6-aminomutase from Clostridium sticklandii
J. Biol. Chem.
275
106-114
2000
Acetoanaerobium sticklandii
Berkovitch, F.; Behshad, E.; Tang, K.H.; Enns, E.A.; Frey, P.A.; Drennan, C.L.
A locking mechanism preventing radical damage in the absence of substrate, as revealed by the X-ray structure of lysine 5,6-aminomutase
Proc. Natl. Acad. Sci. USA
101
15870-15875
2004
Acetoanaerobium sticklandii
Tseng, C.H.; Yang, C.H.; Lin, H.J.; Wu, C.; Chen, H.P.
The S subunit of D-ornithine aminomutase from Clostridium sticklandii is responsible for the allosteric regulation in D-alpha-lysine aminomutase
FEMS Microbiol. Lett.
274
148-153
2007
Acetoanaerobium sticklandii
Maity, A.N.; Hsieh, C.P.; Huang, M.H.; Chen, Y.H.; Tang, K.H.; Behshad, E.; Frey, P.A.; Ke, S.C.
Evidence for conformational movement and radical mechanism in the reaction of 4-thia-L-lysine with lysine 5,6-aminomutase
J. Phys. Chem. B
113
12161-12163
2009
Acetoanaerobium sticklandii
Frey, P.A.; Reed, G.H.
Pyridoxal-5'-phosphate as the catalyst for radical isomerization in reactions of PLP-dependent aminomutases
Biochim. Biophys. Acta
1814
1548-1557
2011
Porphyromonas gingivalis, Acetoanaerobium sticklandii
Maity, A.; Ke, S.
5-Fluorolysine as alternative substrate of lysine 5,6-aminomutase: A computational study
Comp. Theoret. Chem.
1022
1-5
2013
Acetoanaerobium sticklandii
-
Maity, A.N.; Chen, Y.H.; Ke, S.C.
Large-scale domain motions and pyridoxal-5-phosphate assisted radical catalysis in coenzyme B12-dependent aminomutases
Int. J. Mol. Sci.
15
3064-3087
2014
Porphyromonas gingivalis, Acetoanaerobium sticklandii
Chen, Y.H.; Maity, A.N.; Pan, Y.C.; Frey, P.A.; Ke, S.C.
Radical stabilization is crucial in the mechanism of action of lysine 5,6-aminomutase: role of tyrosine-263alpha as revealed by electron paramagnetic resonance spectroscopy
J. Am. Chem. Soc.
133
17152-17155
2011
Acetoanaerobium sticklandii
Chen, Y.H.; Maity, A.N.; Frey, P.A.; Ke, S.C.
Mechanism-based inhibition reveals transitions between two conformational states in the action of lysine 5,6-aminomutase: a combination of electron paramagnetic resonance spectroscopy, electron nuclear double resonance spectroscopy, and density functional
J. Am. Chem. Soc.
135
788-794
2013
Acetoanaerobium sticklandii, Propionibacterium freudenreichii, Propionibacterium freudenreichii ATCC 9614, Acetoanaerobium sticklandii StadtmanHF
Maity, A.; Lin, H.; Chiang, H.; Lo, H.; Ke, S.
Reaction of pyridoxal-5'-phosphate-N-oxide with lysine 5,6-aminomutase Enzyme flexibility toward cofactor analog
ACS Catal.
5
3093-3099
2015
Acetoanaerobium sticklandii (E3PRJ5 AND E3PRJ4)
-
Lo, H.H.; Lin, H.H.; Maity, A.N.; Ke, S.C.
The molecular mechanism of the open-closed protein conformational cycle transitions and coupled substrate binding, activation and product release events in lysine 5,6-aminomutase
Chem. Commun. (Camb.)
52
6399-6402
2016
Acetoanaerobium sticklandii (E3PRJ5 AND E3PRJ4)
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