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EC Tree
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
malate thiokinase, malate-coa ligase,
more
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Malate thiokinase
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Malyl coenzyme A synthetase
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Malyl-CoA synthetase
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Synthetase, malyl coenzyme A
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ATP + malate + CoA = ADP + phosphate + malyl-CoA
ATP + malate + CoA = ADP + phosphate + malyl-CoA
random site reaction mechanism
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ATP + malate + CoA = ADP + phosphate + malyl-CoA
random site reaction mechanism
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ATP + malate + CoA = ADP + phosphate + malyl-CoA
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Acid-thiol ligation
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malate:CoA ligase (ADP-forming)
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ATP + 2-mercaptosuccinate + CoA
ADP + phosphate + 2-mercaptosuccinyl-CoA
ATP + butyrate + CoA
ADP + phosphate + butyryl-CoA
ATP + DL-isocitrate + CoA
ADP + phosphate + isocitryl-CoA
ATP + malate + CoA
ADP + phosphate + malyl-CoA
ATP + malonate + CoA
ADP + phosphate + malonyl-CoA
ATP + oxalate + CoA
ADP + phosphate + oxalyl-CoA
ATP + oxaloacetate + CoA
ADP + phosphate + oxaloacetyl-CoA
ATP + succinate + CoA
ADP + phosphate + succinyl-CoA
additional information
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ATP + 2-mercaptosuccinate + CoA
ADP + phosphate + 2-mercaptosuccinyl-CoA
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activity is 18% relative to L-malate
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ATP + 2-mercaptosuccinate + CoA
ADP + phosphate + 2-mercaptosuccinyl-CoA
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activity is 18% relative to L-malate
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ATP + butyrate + CoA
ADP + phosphate + butyryl-CoA
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ATP + butyrate + CoA
ADP + phosphate + butyryl-CoA
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ATP + DL-isocitrate + CoA
ADP + phosphate + isocitryl-CoA
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activity is 27% of the activity relative to L-malate
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ATP + DL-isocitrate + CoA
ADP + phosphate + isocitryl-CoA
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activity is 27% of the activity relative to L-malate
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ATP + malate + CoA
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ATP + malate + CoA
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Bacteria PerGlx1
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ATP + malate + CoA
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Methanogenic bacterium
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malate:CoA ligase is involved in glycolate degradation pathway under strict anaerobic conditions
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ATP + malate + CoA
ADP + phosphate + malyl-CoA
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ATP + malate + CoA
ADP + phosphate + malyl-CoA
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ATP + malate + CoA
ADP + phosphate + malyl-CoA
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ATP + malate + CoA
ADP + phosphate + malyl-CoA
Bacteria PerGlx1
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ATP + malate + CoA
ADP + phosphate + malyl-CoA
Methanogenic bacterium
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ATP + malate + CoA
ADP + phosphate + malyl-CoA
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ATP + malate + CoA
ADP + phosphate + malyl-CoA
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r
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ATP + malate + CoA
ADP + phosphate + malyl-CoA
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activity with D-malate is 28% relative to L-malate
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ATP + malate + CoA
ADP + phosphate + malyl-CoA
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ATP + malate + CoA
ADP + phosphate + malyl-CoA
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r
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ATP + malate + CoA
ADP + phosphate + malyl-CoA
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ATP + malate + CoA
ADP + phosphate + malyl-CoA
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activity with D-malate is 28% relative to L-malate
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ATP + malonate + CoA
ADP + phosphate + malonyl-CoA
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ATP + malonate + CoA
ADP + phosphate + malonyl-CoA
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ATP + oxalate + CoA
ADP + phosphate + oxalyl-CoA
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ATP + oxalate + CoA
ADP + phosphate + oxalyl-CoA
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ATP + oxaloacetate + CoA
ADP + phosphate + oxaloacetyl-CoA
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ATP + oxaloacetate + CoA
ADP + phosphate + oxaloacetyl-CoA
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ATP + succinate + CoA
ADP + phosphate + succinyl-CoA
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r
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ATP + succinate + CoA
ADP + phosphate + succinyl-CoA
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activity is 105% relative to L-malate
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ATP + succinate + CoA
ADP + phosphate + succinyl-CoA
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random addition of substrates
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ATP + succinate + CoA
ADP + phosphate + succinyl-CoA
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r
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ATP + succinate + CoA
ADP + phosphate + succinyl-CoA
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random addition of substrates
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ATP + succinate + CoA
ADP + phosphate + succinyl-CoA
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activity is 105% relative to L-malate
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additional information
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arsenoslysis reaction is sequentially ordered, with succinyl-CoA binding prior to arsenate
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additional information
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enzyme catalyzes a slow ATP-ADP exchange reaction which is stimulated by coenzyme A or succinyl-CoA, and a slow succinate-succinyl-CoA exchange reaction, which requires phosphate
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additional information
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arsenolysis reaction
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additional information
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arsenolysis reaction
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additional information
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arsenolysis reaction
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additional information
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arsenoslysis reaction is sequentially ordered, with succinyl-CoA binding prior to arsenate
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additional information
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enzyme catalyzes a slow ATP-ADP exchange reaction which is stimulated by coenzyme A or succinyl-CoA, and a slow succinate-succinyl-CoA exchange reaction, which requires phosphate
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additional information
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arsenolysis reaction
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ATP + malate + CoA
ADP + phosphate + malyl-CoA
ATP + malate + CoA
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ATP + malate + CoA
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Bacteria PerGlx1
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ATP + malate + CoA
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Methanogenic bacterium
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malate:CoA ligase is involved in glycolate degradation pathway under strict anaerobic conditions
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ATP + malate + CoA
ADP + phosphate + malyl-CoA
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ATP + malate + CoA
ADP + phosphate + malyl-CoA
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ATP
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high substrate concentrations of ATP inhibit the enzyme activity
Chromium-ATP
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dead-end inhibitor
Methoxycarbonyl-CoA disulfide
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ATP protects, low concentrations of succinyl-CoA protect, L-malate protects only in absence of added sulfate. The inhibitor produces half-of-the-sites reactivity with respect to enzyme phosphorylation
p-hydroxymercuribenzoate
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phosphate
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product inhibitor
succinyl-CoA
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product inhibitor
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additional information
additional information
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additional information
additional information
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additional information
additional information
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brenda
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brenda
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Bacteria PerGlx1
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brenda
Methanogenic bacterium
coculture of Methanospirillum hungatii strain SK, Acetobacterium woodii, and Desulfovibrio vulgaris strain Marburg
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brenda
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brenda
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brenda
gene ffsA
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brenda
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gene ffsA
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brenda
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MTKA_METEA
Methylorubrum extorquens (strain ATCC 14718 / DSM 1338 / JCM 2805 / NCIMB 9133 / AM1)
390
0
42074
Swiss-Prot
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MTKA_RHILO
Mesorhizobium japonicum (strain LMG 29417 / CECT 9101 / MAFF 303099)
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42482
Swiss-Prot
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MTKB_METEA
Methylorubrum extorquens (strain ATCC 14718 / DSM 1338 / JCM 2805 / NCIMB 9133 / AM1)
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30519
Swiss-Prot
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T1CGE1_9ZZZZ
86
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8782
TrEMBL
other Location (Reliability: 4 )
A0A0D6JJU5_9HYPH
375
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39155
TrEMBL
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K1UJC8_9ZZZZ
62
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6419
TrEMBL
other Location (Reliability: 1 )
M1P103_9ZZZZ
365
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40088
TrEMBL
other Location (Reliability: 1 )
A3RVQ3_RALSU
Ralstonia solanacearum (strain UW551)
339
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36702
TrEMBL
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A0A084G2Z9_PSEDA
323
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33821
TrEMBL
Mitochondrion (Reliability: 1 )
T1BE61_9ZZZZ
63
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6437
TrEMBL
other Location (Reliability: 1 )
E5ASP1_MYCRK
Mycetohabitans rhizoxinica (strain DSM 19002 / CIP 109453 / HKI 454)
394
0
43394
TrEMBL
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255000
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gel filtration, nonphosphorylated enzyme, in presence of 20% sucrose
300000
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gel filtration, nonphosphorylated enzyme, in absence of sucrose
34000
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2 * 34000 (alpha) + 2 * 42500 (beta), SDS-PAGE, the phosphoenzyme has an alpha2beta2 structure
42500
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2 * 34000 (alpha) + 2 * 42500 (beta), SDS-PAGE, the phosphoenzyme has an alpha2beta2 structure
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tetramer
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2 * 34000 (alpha) + 2 * 42500 (beta), SDS-PAGE, the phosphoenzyme has an alpha2beta2 structure
tetramer
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2 * 34000 (alpha) + 2 * 42500 (beta), SDS-PAGE, the phosphoenzyme has an alpha2beta2 structure
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additional information
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the phosphorylated enzyme is acid labile and base stable
854
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37
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70% loss of activity after 10 min
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during purification and storage, the enzyme preparation is supplemented with 50 mM KCl and 1 mM DTT to achieve an optimal stabilization
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rapidly denatured when frozen and thawed one time
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4°C, stable for several weeks
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Ni-NTA column chromatography
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expressed in Escherichia coli BL21(DE3) cells
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Friedrich, M.; Laderer, U.; Schink, B.
Fermentative degradation of glycolic acid by defined synthrophic cocultures
Arch. Microbiol.
156
398-404
1991
Methanogenic bacterium
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brenda
Friedrich, M.; Schink, B.
Fermentative degradation of glyoxylate by a new strictly anaerobic bacterium
Arch. Microbiol.
156
392-397
1991
Bacteria, Bacteria PerGlx1
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brenda
Willibald, B.; Boves, H.; Holler, E.
Preparative synthesis of beta-L-malyl-coenzyme A assisted by malyl-coenzyme A synthetase from Pseudomonas AM1
Anal. Biochem.
227
363-367
1995
Pseudomonas sp., Pseudomonas sp. AM1(2006)
brenda
Surendranathan, K.K.; Hersch, L.B.
Malate thiokinase. Evidence for a random site reaction mechanism
J. Biol. Chem.
258
3794-3798
1983
Pseudomonas sp., Pseudomonas sp. AM1(2006)
brenda
Hersh, L.B.; Surendranathan, K.K.
Reaction of malate thiokinase with methoxycarbonyl-CoA disulfide
J. Biol. Chem.
257
11633-11638
1982
Pseudomonas sp.
brenda
Hersh, L.B.; Peet, M.
Half-of-the-sites reactivity in the malate thiokinase reaction
J. Biol. Chem.
256
1732-1737
1981
Pseudomonas sp., Pseudomonas sp. MA
brenda
Elwell,M.; Hersh, L.B.
Substrate-dependent dissociation of malate thiokinase
J. Biol. Chem.
254
2434-2438
1979
Pseudomonas sp., Pseudomonas sp. MA
brenda
Hersh, L.B.
Malate thiokinase. The reaction mechanism as determined by initial rate studies
J. Biol. Chem.
249
6264-6271
1974
Pseudomonas sp., Pseudomonas sp. MA
brenda
Hersh, L.B.
Malate adenosine triphosphate lyase. Separation of the reaction into a malate thiokinase and malyl coenzyme A lyase
J. Biol. Chem.
248
7295-7303
1973
Pseudomonas sp., Pseudomonas sp. MA
brenda
Wu, X.; Zhou, F.; Tu, G.; Zou, X.
Gene cloning, expression and characterization of malate-CoA ligase in the polymerization pathway of polymalic acid from Aureobasidium pullulans
Acta Microbiol. Sin.
54
919-925
2014
Aureobasidium pullulans, Aureobasidium pullulans CCTCC M2012223
brenda
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