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EC Tree
The expected taxonomic range for this enzyme is: Bacteria, Archaea
Synonyms
2-methyleneglutarate mutase, alpha-methyleneglutarate mutase,
more
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alpha-Methyleneglutarate mutase
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Mutase, 2-methyleneglutarate
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2-Methyleneglutarate = 2-methylene-3-methylsuccinate
2-Methyleneglutarate = 2-methylene-3-methylsuccinate
mechanism
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2-Methyleneglutarate = 2-methylene-3-methylsuccinate
the steric course of the reaction is such that the acrylyl residue migrates from the beta-carbon to the alpha-carbon of the propionate with inversion of configuration at the alpha-carbon
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2-Methyleneglutarate = 2-methylene-3-methylsuccinate
the enzyme catalyzes the reversible migration of an acryloyl residue from the alpha-carbon to the beta-carbon of propionate with inversion of configuration at the alpha-carbon
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2-Methyleneglutarate = 2-methylene-3-methylsuccinate
unimolecular free radical rearrangement via 3-butenyl and cyclopropylmethyl intermediates is a reasonable mechanism for the rearrangement step of the enzyme
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2-Methyleneglutarate = 2-methylene-3-methylsuccinate
mechanism via protein-bound free radicals
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2-Methyleneglutarate = 2-methylene-3-methylsuccinate
rotation of the exo-methylene group of 2-methyleneglutarate
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2-Methyleneglutarate = 2-methylene-3-methylsuccinate
formation of an unusual oxygen-sensitive Co(II) species during catalysis
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2-Methyleneglutarate = 2-methylene-3-methylsuccinate
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group transfer
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intramolecular
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2-methyleneglutarate carboxy-methylenemethylmutase
Requires a cobamide coenzyme.
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(R)-3-[methyl-H3]methylitaconate
2-methyleneglutarate
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r
(R,Z)-3-methyl[2'-H1]itaconate
2-methyleneglutarate
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r
(R,Z)-3-[methyl-H3]methyl[2'-H1]itaconate
2-methyleneglutarate
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r
2-methyleneglutarate
(R)-3-methylitaconate
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r
2-Methyleneglutarate
2-Methylene-3-methylsuccinate
2-methylene[4-H2]glutarate
(R)-3-methylitaconate
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r
additional information
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2-Methyleneglutarate
2-Methylene-3-methylsuccinate
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2-Methyleneglutarate
2-Methylene-3-methylsuccinate
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2-Methyleneglutarate
2-Methylene-3-methylsuccinate
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2-Methyleneglutarate
2-Methylene-3-methylsuccinate
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2-Methyleneglutarate
2-Methylene-3-methylsuccinate
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2-Methyleneglutarate
2-Methylene-3-methylsuccinate
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2-Methyleneglutarate
2-Methylene-3-methylsuccinate
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2-Methyleneglutarate
2-Methylene-3-methylsuccinate
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2-Methyleneglutarate
2-Methylene-3-methylsuccinate
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i.e methylitaconate
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2-Methyleneglutarate
2-Methylene-3-methylsuccinate
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r
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2-Methyleneglutarate
2-Methylene-3-methylsuccinate
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r
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2-Methyleneglutarate
2-Methylene-3-methylsuccinate
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r
i.e methylitaconate
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2-Methyleneglutarate
2-Methylene-3-methylsuccinate
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r
i.e methylitaconate
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2-Methyleneglutarate
2-Methylene-3-methylsuccinate
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the equilibrium favours the formation of 2-methyleneglutarate
i.e methylitaconate
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additional information
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inducible enzyme, participates in the anaerobic conversion of nicotinic acid to equimolar amounts of propionate
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additional information
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enzyme is induced by growth on nicotinic acid and is not detectable in cells grown on glucose
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additional information
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carbon-skeleton rearrangement mechanism. Adenosylcobalamin acts as a carrier for the hydrogen atom that is abstracted from alpha-methyleneglutarate and replaced by the acrylyl group of 2-methyleneglutarate
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additional information
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additional information
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inducible enzyme, participates in the anaerobic conversion of nicotinic acid to equimolar amounts of propionate
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additional information
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enzyme is induced by growth on nicotinic acid and is not detectable in cells grown on glucose
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additional information
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carbon-skeleton rearrangement mechanism. Adenosylcobalamin acts as a carrier for the hydrogen atom that is abstracted from alpha-methyleneglutarate and replaced by the acrylyl group of 2-methyleneglutarate
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cobamide
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required
cobamide
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the enzyme contains adenosylcobalamin and varying amounts of oxygen-stable cob(II)alamin. The content of total cobalamin is 2-4 mol/ml enzyme, the content of cob(II)alamin is 6-11% of the total cobalamin. The oxygen-stable cob(II)alamin is not involved in catalysis
cobamide
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acts as a carrier for the hydrogen atom that is abstracted from alpha-methyleneglutarate. The enzyme contains 4 cobalamin molecules per tetramer. The cobalamins consist of adenosylcobalamin and cobalamin(II). Enzyme containing adenosylcobalamin is the active form of the enzyme but the enzyme containing cobalamin(II) is stable to oxygen and is an inactive form of the enzyme
cobamide
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e.g. alpha-(5,6-dimethylbenzimidazolyl)cobamide coenzyme, Km: 0.000073 mM, alpha-(benzimidazolyl)-cobamide coenzyme, Km: 0.0003 mM, or alpha-(adenyl)-cobamide coenzyme, Km: 0.00125 mM. The most effective coenzyme is alpha(5,6-dimethylbenzimidazolyl)-cobamide coenzyme
vitamin B12
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vitamin B12
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dependent on
vitamin B12
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contains 2.1 mol of this coenzyme per homotetramer
vitamin B12
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during catalysis the Co-C bond of the coenzyme is cleaved
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(Z)-glutaconate
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mechanism-based inactivation. Inhibitor induces homolysis of the Co-C bond of coenzyme B12 to afford cob(II)alamin and the 5'-deoxyadenosyl radical. The 5'-deoxyadenosyl radical adds to the double bond of (Z)-glutaconate to afford a radical adduct and subsequent formation of aquocobalamin
1-Methyl-1,2-cis-cyclopropanedicarboxylate
1-Methyl-1,2-trans-cyclopropanedicarboxylate
1-methylcyclopropane-(1R,2R)-dicarboxylate
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weak noncompetitive
buta-1,3-diene-2,3-dicarboxylate
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mechanism-based inactivation. Inhibitor induces homolysis of the Co-C bond of coenzyme B12 to afford cob(II)alamin and the 5'-deoxyadenosyl radical. The 5'-deoxyadenosyl radical adds to a double bond of buta-1,3-diene-2,3-dicarboxylate to afford a relatively stable radical adduct in the active site of the enzyme
p-chloromercuriphenylsulfonic acid
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1-Methyl-1,2-cis-cyclopropanedicarboxylate
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noncompetitive, slight inhibitor
1-Methyl-1,2-cis-cyclopropanedicarboxylate
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1-Methyl-1,2-cis-cyclopropanedicarboxylate
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noncompetitive, slight inhibitor
1-Methyl-1,2-trans-cyclopropanedicarboxylate
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competitive
1-Methyl-1,2-trans-cyclopropanedicarboxylate
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1-Methyl-1,2-trans-cyclopropanedicarboxylate
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competitive
glutaconate
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noncompetitive
glutaconate
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noncompetitive
iodoacetamide
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alkylated enzyme
Itaconate
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competitive
mesaconate
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competitive
succinate
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competitive
additional information
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the enzyme is inactivated by light of the wavelength, lambda = 620 nm. Reactivation of up to 50% of the activity is achieved by incubation with coenzyme B12 and dithiothreitol, the substrates 2-methgyleneglutarate or 3-methylitaconate specifically protect the enzyme from inactivation by visible light
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additional information
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acrylate and 2-methylpent-2-enedioate are noninhibitory
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sulfhydryl groups
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the enzyme is a sulfhydryl protein
sulfhydryl groups
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contains active thiol groups
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0.4
(R)-3-methylitaconate
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pH 7.4
0.38
(R)-3-[methyl-H3]methylitaconate
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pH 7.4
3.1 - 7.1
2-Methyleneglutarate
2.3
2-methylene[4-H2]glutarate
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pH 7.4
3.1
2-Methyleneglutarate
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pH 7.4
4
2-Methyleneglutarate
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7.1
2-Methyleneglutarate
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18
(R)-3-methylitaconate
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pH 7.4
1.1
(R)-3-[methyl-H3]methylitaconate
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pH 7.4
17
(R,Z)-3-methyl[2'-H1]itaconate
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pH 7.4
1.4
(R,Z)-3-[methyl-H3]methyl[2'-H1]itaconate
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pH 7.4
30
2-Methyleneglutarate
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pH 7.4
2.3
2-methylene[4-H2]glutarate
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pH 7.4
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13
1-methylcyclopropane-(1R,2R)-dicarboxylate
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0.51
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preparation which is heavily contaminated with methylitaconate isomerase
additional information
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additional information
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additional information
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additional information
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continuous spectrophotometric assay
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7.5 - 8
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sharp decrease in activity below pH 7.5 and above pH 8
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2986 , 2988 , 3453 , 3522 , 3524 , 3526 , 3527 , 3528 , 3529 , 3530 , 3531 , 3532 , 651581 , 661159 , 679646 -
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brenda
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MGM_EUBBA
614
0
66750
Swiss-Prot
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A0A4Y7RE17_9FIRM
618
0
67215
TrEMBL
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F6EZU6_SPHCR
717
0
77859
TrEMBL
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A0A212M107_9FIRM
uncultured Sporomusa sp
618
0
67184
TrEMBL
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A6NVP6_9FIRM
619
0
68239
TrEMBL
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A0A259ULC8_9FIRM
615
0
67428
TrEMBL
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F4LUN5_TEPAE
Tepidanaerobacter acetatoxydans (strain DSM 21804 / JCM 16047 / Re1)
615
0
68265
TrEMBL
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A0A1U7MCQ3_9FIRM
618
0
67165
TrEMBL
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A0A517DYQ5_9FIRM
615
0
67272
TrEMBL
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B0PCL9_9FIRM
621
0
68261
TrEMBL
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A0A6I5ZNC7_9THEO
617
0
66972
TrEMBL
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A0A1J5JE45_MOOTH
617
0
66798
TrEMBL
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A0A259UP89_9FIRM
615
0
66616
TrEMBL
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A0A3F3S1T4_9FIRM
252
0
27434
TrEMBL
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C3MJF2_SULIL
Sulfolobus islandicus (strain L.S.2.15 / Lassen #1)
141
0
15272
TrEMBL
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A0A174RB23_9FIRM
621
0
68280
TrEMBL
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A0A1M4M2U6_9FIRM
619
0
68313
TrEMBL
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A0A1C5ZX70_9FIRM
uncultured Flavonifractor sp
619
0
68207
TrEMBL
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B2A7L4_NATTJ
Natranaerobius thermophilus (strain ATCC BAA-1301 / DSM 18059 / JW/NM-WN-LF)
616
0
68494
TrEMBL
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A0A0E0URI2_SINMB
Sinorhizobium meliloti (strain BL225C)
712
0
77533
TrEMBL
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A0A0S1XBP3_THEBA
143
0
15570
TrEMBL
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170000
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sucrose density gradient centrifugation
300000
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gel filtration, sucrose density gradient centrifugation, nondenaturing PAGE
67000
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alpha4, 4 * 67000
70000
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4 * 70000, SDS-PAGE
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tetramer
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4 * 70000, SDS-PAGE
tetramer
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alpha4, 4 * 67000
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D483N
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0.06%of wild-type activity
H464Q
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35% of wild-type activity
H485Q
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less than 0.03% of wild-type activity
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enzyme rapidly decays, when stored at low protein concentrations, 1 mg/ml. Complete loss of activity after 3 days at 0°C and 38% loss of activity after 6 days at -80°C
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enzyme containing cobalamin(II) is stable to oxygen and is an inactive form of the enzyme
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3526
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-80°C, protein concentration 1 mg/ml, 38% loss of activity after 6 days
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-80°C, protein concentration 10 mg/ml, about 10% loss of activity after 6 months
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0°C, protein concentration 1 mg/ml, complete loss of activity after 3 days
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overexpression in Escherichia coli
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denaturation with 8 M urea in the presence of 2 mM dithiothreitol followed by gel chromatography and renaturation affords an inactive enzyme which contains 40-50% of the initially bound cobalamin
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Kung, H.F.; Tsai, L.
Nicotinic acid metabolism. VII. Mechanism of action of Clostridial alpha-methyleneglutarate mutase (B12-dependent) and methylitaconate isomerase
J. Biol. Chem.
246
6436-6443
1971
Eubacterium barkeri
brenda
Hartrampf, G.; Buckel, W.
On the steric course of the adenosylcobalamin-dependent 2-methyleneglutarate mutase reaction in Clostridium barkeri
Eur. J. Biochem.
156
301-304
1986
Eubacterium barkeri
brenda
Barker, H.A.
Coenzyme B12-dependent mutases causing carbon chain rearrangements
The Enzymes, 3rd Ed. (Boyer, P. D. , ed. )
6
509-537
1972
Eubacterium barkeri
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brenda
Kung, H.F.; Stadtman, T.C.
Nicotinic acid metabolism. VI. Purification and properties of alpha-methyleneglutarate mutase (B12-dependent) and methylitaconate isomerase
J. Biol. Chem.
246
3378-3388
1971
Eubacterium barkeri
brenda
Edwards, C.H.; Golding, B.T.
Rotation of the exo-methylene group of 2-methyleneglutarate catalyzed by coenzyme B12-dependent 2-methyleneglutarate mutase from Clostridium barkeri
J. Am. Chem. Soc.
118
4192-4193
1996
Eubacterium barkeri
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brenda
Chemaly, S.M.
alpha-Methyleneglutarate mutase: an adenosylcobalamin-dependent enzyme
S. Afr. J. Chem.
47
37-47
1994
Eubacterium barkeri
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brenda
Michel, C.; Hartrampf, G.; Buckel, W.
Assay and purification of the adenosylcobalamin-dependent 2-methyleneglutarate mutase from Clostridium barkeri
Eur. J. Biochem.
184
103-107
1989
Eubacterium barkeri
brenda
Ashwell, S.; Davies, A.G.; Golding, B.T.; Hay-Motherwell, R.; Mwesigye-Kibende, S.
Model experiments pertaining to the mechanism of action of vitamin B12-dependent alpha-methyleneglutarate mutase
J. Chem. Soc. Chem. Commun.
1989
1483-1485
1989
Eubacterium barkeri
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brenda
Zelder, O.; Buckel, W.
On the role of two different cobalt(II) species in coenzyme B12-dependent 2-methyleneglutarate mutase from Clostridium barkeri
Biol. Chem. Hoppe-Seyler
374
85-90
1993
Eubacterium barkeri
brenda
Michel, C.; Buckel, W.
Purification of the coenzyme B12-containing 2-methyleneglutarate mutase from Clostridium barkeri by high-performance liquid chromatography
J. Chromatogr.
587
93-99
1991
Eubacterium barkeri
brenda
Michel, C.; Buckel, W.
Coenzyme B12-dependent 2-methylenenglutarate mutase from Clostridium barkeri
FEBS Lett.
281
108-110
1991
Eubacterium barkeri
brenda
Michel, C.; Albracht, S.P.J.; Buckel, W.
Adenosylcobalamin and cob(II)alamin as prosthetic groups of 2-methyleneglutarate mutase from Clostridium barkeri
Eur. J. Biochem.
205
767-773
1992
Eubacterium barkeri
brenda
Pierik, A.J.; Ciceri, D.; Broker, G.; Edwards, C.H.; McFarlane, W.; Winter, J.; Buckel, W.; Golding, B.T.
Rotation of the exo-methylene group of (R)-3-methylitaconate catalyzed by coenzyme B(12)-dependent 2-methyleneglutarate mutase from Eubacterium barkeri
J. Am. Chem. Soc.
124
14039-14048
2002
Eubacterium barkeri
brenda
Pierik, A.J.; Ciceri, D.; Lopez, R.F.; Kroll, F.; Broker, G.; Beatrix, B.; Buckel, W.; Golding, B.T.
Searching for intermediates in the carbon skeleton rearrangement of 2-methyleneglutarate to (R)-3-methylitaconate catalyzed by coenzyme B12-dependent 2-methyleneglutarate mutase from Eubacterium barkeri
Biochemistry
44
10541-10551
2005
Eubacterium barkeri
brenda
Buckel, W.; Pierik, A.J.; Plett, S.; Alhapel, A.; Suarez, D.; Tu, S.; Golding, B.T.
Mechanism-based inactivation of coenzyme B12-dependent 2-methyleneglutarate mutase by (Z)-glutaconate and buta-1,3-diene-2,3-dicarboxylate
Eur. J. Inorg. Chem.
2006
3622-3626
2006
Eubacterium barkeri
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brenda
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