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(S)-methylmalonyl-CoA + pyruvate
propanoyl-CoA + oxaloacetate
3-fluoropropionyl-CoA + oxaloacetate
acrylyl-CoA + pyruvate + F- + CO2
-
no F-release if pyruvate or malate are substituted for oxaloacetate
-
?
acetoacetyl-CoA + oxaloacetate
3-oxoglutaryl-CoA + pyruvate
acetyl-CoA + oxaloacetate
malonyl-CoA + pyruvate
butyryl-CoA + oxaloacetate
ethylmalonyl-CoA + pyruvate
propionyl-CoA + oxaloacetate
(S)-methylmalonyl-CoA + pyruvate
additional information
?
-
(S)-methylmalonyl-CoA + pyruvate
propanoyl-CoA + oxaloacetate
-
-
-
-
?
(S)-methylmalonyl-CoA + pyruvate
propanoyl-CoA + oxaloacetate
-
-
-
-
r
(S)-methylmalonyl-CoA + pyruvate
propanoyl-CoA + oxaloacetate
-
-
-
-
?
(S)-methylmalonyl-CoA + pyruvate
propanoyl-CoA + oxaloacetate
-
-
-
-
?
(S)-methylmalonyl-CoA + pyruvate
propanoyl-CoA + oxaloacetate
-
-
-
-
r
(S)-methylmalonyl-CoA + pyruvate
propanoyl-CoA + oxaloacetate
-
-
-
-
r
acetoacetyl-CoA + oxaloacetate
3-oxoglutaryl-CoA + pyruvate
-
-
-
?
acetoacetyl-CoA + oxaloacetate
3-oxoglutaryl-CoA + pyruvate
-
-
-
?
acetoacetyl-CoA + oxaloacetate
3-oxoglutaryl-CoA + pyruvate
-
carboxylation at about 2.5% the rate of propionyl-CoA
-
?
acetyl-CoA + oxaloacetate
malonyl-CoA + pyruvate
-
-
-
?
acetyl-CoA + oxaloacetate
malonyl-CoA + pyruvate
-
-
-
-
?
acetyl-CoA + oxaloacetate
malonyl-CoA + pyruvate
-
-
-
?
acetyl-CoA + oxaloacetate
malonyl-CoA + pyruvate
-
carboxylation at about 50% the rate of propionyl-CoA
-
r
acetyl-CoA + oxaloacetate
malonyl-CoA + pyruvate
-
-
-
?
butyryl-CoA + oxaloacetate
ethylmalonyl-CoA + pyruvate
-
-
-
?
butyryl-CoA + oxaloacetate
ethylmalonyl-CoA + pyruvate
-
-
-
-
?
butyryl-CoA + oxaloacetate
ethylmalonyl-CoA + pyruvate
-
-
-
?
butyryl-CoA + oxaloacetate
ethylmalonyl-CoA + pyruvate
-
carboxylation at about 10% the rate of propionyl-CoA
-
?
propionyl-CoA + oxaloacetate
(S)-methylmalonyl-CoA + pyruvate
-
-
-
r
propionyl-CoA + oxaloacetate
(S)-methylmalonyl-CoA + pyruvate
-
-
-
r
propionyl-CoA + oxaloacetate
(S)-methylmalonyl-CoA + pyruvate
-
-
-
r
propionyl-CoA + oxaloacetate
(S)-methylmalonyl-CoA + pyruvate
-
-
-
r
propionyl-CoA + oxaloacetate
(S)-methylmalonyl-CoA + pyruvate
-
-
-
r
propionyl-CoA + oxaloacetate
(S)-methylmalonyl-CoA + pyruvate
-
spontaneous decarboxylation follows
-
r
propionyl-CoA + oxaloacetate
(S)-methylmalonyl-CoA + pyruvate
-
two partial reactions
-
r
propionyl-CoA + oxaloacetate
(S)-methylmalonyl-CoA + pyruvate
-
two partial reactions
-
r
propionyl-CoA + oxaloacetate
(S)-methylmalonyl-CoA + pyruvate
-
two partial reactions
-
r
propionyl-CoA + oxaloacetate
(S)-methylmalonyl-CoA + pyruvate
-
two partial reactions
-
r
propionyl-CoA + oxaloacetate
(S)-methylmalonyl-CoA + pyruvate
-
two partial reactions
-
r
propionyl-CoA + oxaloacetate
(S)-methylmalonyl-CoA + pyruvate
-
two partial reactions
-
r
propionyl-CoA + oxaloacetate
(S)-methylmalonyl-CoA + pyruvate
-
two partial reactions
-
r
propionyl-CoA + oxaloacetate
(S)-methylmalonyl-CoA + pyruvate
-
two partial reactions
-
r
propionyl-CoA + oxaloacetate
(S)-methylmalonyl-CoA + pyruvate
-
two partial reactions
-
r
propionyl-CoA + oxaloacetate
(S)-methylmalonyl-CoA + pyruvate
-
-
-
r
propionyl-CoA + oxaloacetate
(S)-methylmalonyl-CoA + pyruvate
-
-
enzyme specific for the S isomer
r
propionyl-CoA + oxaloacetate
(S)-methylmalonyl-CoA + pyruvate
-
-
-
?
propionyl-CoA + oxaloacetate
(S)-methylmalonyl-CoA + pyruvate
-
-
-
?
propionyl-CoA + oxaloacetate
(S)-methylmalonyl-CoA + pyruvate
-
-
-
r
additional information
?
-
-
-
-
-
?
additional information
?
-
-
structural requirements of the C1-donor: carbonyl group in beta-position to carboxyl group being donated and adjacent either to another carboxyl group or to coenzyme A
-
-
?
additional information
?
-
-
structural requirements of the C1-donor: carbonyl group in beta-position to carboxyl group being donated and adjacent either to another carboxyl group or to coenzyme A
-
-
?
additional information
?
-
-
2-oxobutyrate, 2-oxovalerate, 2-oxoglutarate, 3-oxoglutarate cannot replace pyruvate and is no C1-donor
-
-
?
additional information
?
-
-
enzyme catalyses the formation of the precursor of tylosin, protylonoide
-
-
?
additional information
?
-
-
enzyme involved in the biosynthesis of the tylosin
-
-
?
additional information
?
-
-
enzyme catalyses the formation of the precursor of tylosin, protylonoide
-
-
?
additional information
?
-
-
enzyme involved in the biosynthesis of the tylosin
-
-
?
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?
-
x * 55620, calculated, x * 55623, ESI-MS, x * 55500, SDS-PAGE of 5S subunit
dimer
crystallization data
hexamer
crystallization data
multimer
-
-
multimer
-
the central cylindrical hexameric 12S subunit, the outer six dimeric 5S subunit, and the twelve 1.3S linkers
additional information
-
existence of a novel, previously unidentified subunit, a assemply-promoting factor, APF, which is nessessary for the assemply of enzyme, MW: 60000 Da, SDS-PAGE
additional information
-
structure
additional information
-
MW of 12S hexamer: 338000Da
additional information
-
amino acid sequence of biotinyl subunit
additional information
-
amino acid sequence of biotinyl subunit
additional information
-
amino acid sequence of biotinyl subunit
additional information
-
the 26S holoenzyme consists of a hexameric central 12S subunit, 360000 Da and six peripheral dimeric 5S subunits, 6 * 120000 Da each of which is linked to the central subunit by 2 biotinyl 1.3S subunits, 12 * MW 12000
additional information
-
the 26S holoenzyme consists of a hexameric central 12S subunit, 360000 Da and six peripheral dimeric 5S subunits, 6 * 120000 Da each of which is linked to the central subunit by 2 biotinyl 1.3S subunits, 12 * MW 12000
additional information
-
the 26S holoenzyme consists of a hexameric central 12S subunit, 360000 Da and six peripheral dimeric 5S subunits, 6 * 120000 Da each of which is linked to the central subunit by 2 biotinyl 1.3S subunits, 12 * MW 12000
additional information
-
the 26S holoenzyme consists of a hexameric central 12S subunit, 360000 Da and six peripheral dimeric 5S subunits, 6 * 120000 Da each of which is linked to the central subunit by 2 biotinyl 1.3S subunits, 12 * MW 12000
additional information
-
the 26S holoenzyme consists of a hexameric central 12S subunit, 360000 Da and six peripheral dimeric 5S subunits, 6 * 120000 Da each of which is linked to the central subunit by 2 biotinyl 1.3S subunits, 12 * MW 12000
additional information
-
the 26S holoenzyme consists of a hexameric central 12S subunit, 360000 Da and six peripheral dimeric 5S subunits, 6 * 120000 Da each of which is linked to the central subunit by 2 biotinyl 1.3S subunits, 12 * MW 12000
additional information
-
the 26S holoenzyme consists of a hexameric central 12S subunit, 360000 Da and six peripheral dimeric 5S subunits, 6 * 120000 Da each of which is linked to the central subunit by 2 biotinyl 1.3S subunits, 12 * MW 12000
additional information
-
the 26S holoenzyme consists of a hexameric central 12S subunit, 360000 Da and six peripheral dimeric 5S subunits, 6 * 120000 Da each of which is linked to the central subunit by 2 biotinyl 1.3S subunits, 12 * MW 12000
additional information
-
5S subunit with a native MW 120000 Da, gel filtration and a subunit MW 60000 Da, SDS-PAGE
additional information
-
5S subunit is a dimer of identical monomers, contains Co2+ and Zn2+ and assembles with two 1.3 subunits to form a stable complex termed the 6S subunit
additional information
-
5S subunit is a dimer of identical monomers, contains Co2+ and Zn2+ and assembles with two 1.3 subunits to form a stable complex termed the 6S subunit
additional information
-
1.3 S is homogen, SDS-PAGE
additional information
-
structure
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Hoffmann, A.; Hilpert, W.; Dimroth, P.
The carboxyltransferase activity of the sodium-ion-translocating methylmalonyl-CoA decarboxylase of Veillonella alcalescens
Eur. J. Biochem.
179
645-650
1989
Veillonella parvula
brenda
Wood, H.G.
Transcarboxylase
The Enzymes, 3rd Ed. (Boyer, P. D. , ed. )
6
83-115
1972
Propionibacterium sp.
-
brenda
Swick, R.W.; Wood, H.G.
The role of transcarboxylase in propionic acid ermentation
Proc. Natl. Acad. Sci. USA
46
28-41
1960
Canis lupus familiaris, Propionibacterium freudenreichii subsp. shermanii, Propionibacterium freudenreichii subsp. shermanii 52W
brenda
Berger, M.; Wood, H.G.
Purification of the subunits of transcarboxylase by affinity chromatography on avidin-sepharose
J. Biol. Chem.
250
927-933
1975
Propionibacterium freudenreichii subsp. shermanii
brenda
Maloy, W.L.; Bowien, B.U.; Zwolinski, G.K.; Kumar, K.G.; Wood, H.G.; Ericsson, L.H.; Walsh, K.A.
Amino acid sequence of the biotinyl subunit from transcarboxylase
J. Biol. Chem.
254
11615-11622
1979
Propionibacterium freudenreichii subsp. shermanii
brenda
Harmon, F.R.; Goss, N.H.; Wood, H.G.
Stabilization of the quaternary structure of transcarboxylase by cobalt (II) ions
Biochemistry
21
2847-2852
1982
Propionibacterium freudenreichii subsp. shermanii
brenda
Stubbe, J.; Fish, S.; Abeles, R.H.
Are carboxylations involving biotin concerted or nonconcerted?
J. Biol. Chem.
255
236-242
1980
Propionibacterium sp.
brenda
Shenoy, B.C.; Xie, Y.; Park, V.L.; Kumar, G.K.; Beegen, H.; Wood, H.G.; Samols, D.
The importance of methionine residues for the catalysis of the biotin enzyme, transcarboxylase. Analysis by site-directed mutagenesis
J. Biol. Chem.
267
18407-18412
1992
Propionibacterium freudenreichii subsp. shermanii
brenda
O'Keefe, S.J.; Knowles, J.R.
Biotin-dependent carboxylation catalyzed by transcarboxylase is a stepwise process [published erratum appears in Biochemistry 1987 Sep 8;26(18):5952]
Biochemistry
25
6077-6084
1986
Propionibacterium freudenreichii subsp. shermanii
brenda
Rivera-Hainaj, R.E.; Pusztai-Carey, M.; Reddy, D.V.; Choowongkomon, K.; Soennichsen, F.D.; Carey, P.R.
Characterization of the carboxylate delivery module of transcarboxylase: following spontaneous decarboxylation of the 1.3S-CO2- subunit by NMR and FTIR spectroscopies
Biochemistry
41
2191-2197
2002
Propionibacterium freudenreichii subsp. shermanii
brenda
Zheng, X.; Rivera-Hainaj, R.E.; Zheng, Y.; Pusztai-Carey, M.; Hall, P.R.; Yee, V.C.; Carey, P.R.
Substrate binding induces a cooperative conformational change in the 12S subunit of transcarboxylase: raman crystallographic evidence
Biochemistry
41
10741-10746
2002
Propionibacterium freudenreichii subsp. shermanii
brenda
Shenoy, B.C.; Kumar, G.K.; Samols, D.
Dissection of the biotinyl subunit of transcarboxylase into regions essential for activity and assembly
J. Biol. Chem.
268
2232-2238
1993
Propionibacterium freudenreichii subsp. shermanii
brenda
Shenoy, B.C.; Magner, W.J.; Kumar, G.K.; Phillips, N.F.B.; Haase, F.C.; Samols, D.
The nonbiotinylated form of the 1.3 S subunit of transcarboxylase binds to avidin (monomeric)-agarose: Purification and separation from the biotinylated 1.3 S subunit
Protein Expr. Purif.
4
85-94
1993
Propionibacterium freudenreichii subsp. shermanii
brenda
Shenoy, B.C.; Samols, D.; Kumar, G.K.
The conserved methionines of the 1.3 S biotinyl subunit of transcarboxylase: effect of mutations on conformation and activity
Arch. Biochem. Biophys.
304
359-366
1993
Propionibacterium freudenreichii subsp. shermanii
brenda
Woo, S.B.; Shenoy, B.C.; Wood, H.G.; Magner, W.J.; Kumar, G.K.; Beegen, H.; Samols, D.
Effect of deletion from the carboxyl terminus of the 12 S subunit on activity of transcarboxylase
J. Biol. Chem.
268
16413-16419
1993
Propionibacterium freudenreichii subsp. shermanii
brenda
Xie, Y.; Shenoy, B.C.; Magner, W.J.; Hejlik, D.P.; Samols, D.
Purification and characterization of the recombinant 5 S subunit of transcarboxylase from Escherichia coli
Protein Expr. Purif.
4
456-464
1993
Propionibacterium freudenreichii subsp. shermanii
brenda
Shenoy, B.C.; Xie, Y.; Sha, D.; Samols, D.
Identification and characterization of a factor which is essential for assembly of transcarboxylase
Biochemistry
32
10750-10756
1993
Propionibacterium freudenreichii subsp. shermanii
brenda
Choi, D.B.; Park, Y.; Okabe, M.
Effects of rapeseed oil on activity of methylmalonyl-CoA carboxyltransferase in culture of Streptomyces fradiae
Biosci. Biotechnol. Biochem.
62
902-906
1998
Streptomyces fradiae, Streptomyces fradiae T1558
brenda
Jank, M.M.; Bokorny, S.; Rohm, K.H.; Berger, S.
Expression and biotinylation of a mutant of the transcarboxylase carrier protein from Propioni shermanii
Protein Expr. Purif.
17
123-127
1999
Propionibacterium freudenreichii subsp. shermanii
brenda
Hall, P.R.; Zheng, R.; Pusztai-Carey, M.; van den Akker, F.; Carey, P.R.; Yee, V.C.
Expression and crystallization of several forms of the Propionibacterium shermanii transcarboxylase 5S subunit
Acta Crystallogr. Sect. D
D60
521-523
2004
Propionibacterium freudenreichii subsp. shermanii
brenda
Hall, P.R.; Wang, Y.F.; Rivera-Hainaj, R.E.; Zheng, X.; Pustai-Carey, M.; Carey, P.R.; Yee, V.C.
Transcarboxylase 12S crystal structure: hexamer assembly and substrate binding to a multienzyme core
EMBO J.
22
2334-2347
2003
Propionibacterium freudenreichii subsp. shermanii (Q8GBW6), Propionibacterium freudenreichii subsp. shermanii
brenda
Hall, P.R.; Zheng, R.; Antony, L.; Pusztai-Carey, M.; Carey, P.R.; Yee, V.C.
Transcarboxylase 5S structures: assembly and catalytic mechanism of a multienzyme complex subunit
EMBO J.
23
3621-3631
2004
Propionibacterium freudenreichii subsp. shermanii (Q70AC7), Propionibacterium freudenreichii subsp. shermanii
brenda
Suwannakham, S.; Yang, S.T.
Enhanced propionic acid fermentation by Propionibacterium acidipropionici mutant obtained by adaptation in a fibrous-bed bioreactor
Biotechnol. Bioeng.
91
325-337
2005
Acidipropionibacterium acidipropionici
brenda
Herve, C.; Fondrevez, M.; Cheron, A.; Barloy-Hubler, F.; Jan, G.
Transcarboxylase mRNA: a marker which evidences P. freudenreichii survival and metabolic activity during its transit in the human gut
Int. J. Food Microbiol.
113
303-314
2007
Propionibacterium freudenreichii
brenda
Kumar Bhat, R.; Berger, S.
New and easy strategy for cloning, expression, purification, and characterization of the 5S subunit of transcarboxylase from Propionibacterium f. shermanii
Prep. Biochem. Biotechnol.
37
13-26
2007
Propionibacterium freudenreichii subsp. shermanii
brenda
Yamada, M.; Natsume, R.; Nakamatsu, T.; Horinouchi, S.; Kawasaki, H.; Senda, T.
Crystallization and preliminary crystallographic analysis of DtsR1, a carboxyltransferase subunit of acetyl-CoA carboxylase from Corynebacterium glutamicum
Acta Crystallogr. Sect. F
63
120-122
2007
Corynebacterium glutamicum
brenda
Bhat, R.K.; Berger, S.
The 5S subunit of transcarboxylase interacts with free biotin as studied by transferred-NOESY and Saturation Transfer Difference NMR
Protein Pept. Lett.
15
624-629
2008
Propionibacterium freudenreichii subsp. shermanii
brenda
Jia, Y.; Zhong, J.J.
Enhanced production of ansamitocin P-3 by addition of Mg2+ in fermentation of Actinosynnema pretiosum
Biores. Technol.
102
10147-10150
2011
Actinosynnema pretiosum, Actinosynnema pretiosum ATCC 31565
brenda
Wang, Z.; Lin, M.; Wang, L.; Ammar, E.; Yang, S.
Metabolic engineering of Propionibacterium freudenreichii subsp. shermanii for enhanced propionic acid fermentation: Effects of overexpressing three biotin-dependent carboxylases
Process Biochem.
50
194-204
2015
Propionibacterium freudenreichii, Propionibacterium freudenreichii DSM 4902
-
brenda
Shin, K.S.; Lee, S.K.
Introduction of an acetyl-CoA carboxylation bypass into Escherichia coli for enhanced free fatty acid production
Biores. Technol.
245
1627-1633
2017
Propionibacterium freudenreichii subsp. shermanii, Propionibacterium freudenreichii subsp. shermanii KCTC5753
brenda