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(E)-4-(trimethylammonio)but-2-enoyl-CoA + L-carnitine = (E)-4-(trimethylammonio)but-2-enoate + L-carnitinyl-CoA
4-trimethylammoniobutanoyl-CoA + L-carnitine = 4-trimethylammoniobutanoate + L-carnitinyl-CoA
(E)-4-(trimethylammonio)but-2-enoyl-CoA + L-carnitine = (E)-4-(trimethylammonio)but-2-enoate + L-carnitinyl-CoA
(1)
(E)-4-(trimethylammonio)but-2-enoyl-CoA + L-carnitine = (E)-4-(trimethylammonio)but-2-enoate + L-carnitinyl-CoA
sequential bisubstrate mechanism
(E)-4-(trimethylammonio)but-2-enoyl-CoA + L-carnitine = (E)-4-(trimethylammonio)but-2-enoate + L-carnitinyl-CoA
sequential bisubstrate mechanism
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(E)-4-(trimethylammonio)but-2-enoyl-CoA + L-carnitine = (E)-4-(trimethylammonio)but-2-enoate + L-carnitinyl-CoA
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4-trimethylammoniobutanoyl-CoA + L-carnitine = 4-trimethylammoniobutanoate + L-carnitinyl-CoA
(2)
4-trimethylammoniobutanoyl-CoA + L-carnitine = 4-trimethylammoniobutanoate + L-carnitinyl-CoA
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(E)-4-(trimethylammonio)but-2-enoyl-CoA + L-carnitine
(E)-4-(trimethylammonio)but-2-enoate + L-carnitinyl-CoA
4-trimethylammoniobutanoyl-CoA + L-carnitine
4-trimethylammoniobutanoate + L-carnitinyl-CoA
crotonobetainyl-CoA + L-carnitine
crotonobetaine + L-carnitinyl-CoA
gamma-butyrobetainyl-CoA + L-carnitine
gamma-butyrobetaine + L-carnitinyl-CoA
additional information
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(E)-4-(trimethylammonio)but-2-enoyl-CoA + L-carnitine
(E)-4-(trimethylammonio)but-2-enoate + L-carnitinyl-CoA
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(E)-4-(trimethylammonio)but-2-enoyl-CoA + L-carnitine
(E)-4-(trimethylammonio)but-2-enoate + L-carnitinyl-CoA
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(E)-4-(trimethylammonio)but-2-enoyl-CoA + L-carnitine
(E)-4-(trimethylammonio)but-2-enoate + L-carnitinyl-CoA
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4-trimethylammoniobutanoyl-CoA + L-carnitine
4-trimethylammoniobutanoate + L-carnitinyl-CoA
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4-trimethylammoniobutanoyl-CoA + L-carnitine
4-trimethylammoniobutanoate + L-carnitinyl-CoA
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4-trimethylammoniobutanoyl-CoA + L-carnitine
4-trimethylammoniobutanoate + L-carnitinyl-CoA
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crotonobetainyl-CoA + L-carnitine
crotonobetaine + L-carnitinyl-CoA
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crotonobetainyl-CoA + L-carnitine
crotonobetaine + L-carnitinyl-CoA
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crotonobetainyl-CoA + L-carnitine
crotonobetaine + L-carnitinyl-CoA
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gamma-butyrobetainyl-CoA + L-carnitine
gamma-butyrobetaine + L-carnitinyl-CoA
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gamma-butyrobetainyl-CoA + L-carnitine
gamma-butyrobetaine + L-carnitinyl-CoA
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gamma-butyrobetainyl-CoA + L-carnitine
gamma-butyrobetaine + L-carnitinyl-CoA
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additional information
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enzyme exhibits high cosubstrate specificity to CoA derivatives of trimethylammonium compounds. Hydration of crotonobetaine to L-carnitine proceeds at the CoA level in two steps: the CaiD catalyzed hydration of crotonobetainyl-CoA to L-carnitinyl-CoA, followed by a CoA transfer from L-carnitinyl-CoA to crotonobetaine, catalyzed by transferase CaiB. When gamma-butyrobetainyl-CoA is used as a cosubstrate, the first reaction is the CoA transfer. The optimal ratios of CaiB and CaiD during this hydration reaction, determined to be 4:1 when crotonobetainyl-CoA is used as cosubstrate and 5:1 when gamma-butyrobetainyl-CoA is used as cosubstrate, are different from that found for in vivo conditions, i.e. 1:3
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additional information
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enzyme exhibits high cosubstrate specificity to CoA derivatives of trimethylammonium compounds. Hydration of crotonobetaine to L-carnitine proceeds at the CoA level in two steps: the CaiD catalyzed hydration of crotonobetainyl-CoA to L-carnitinyl-CoA, followed by a CoA transfer from L-carnitinyl-CoA to crotonobetaine, catalyzed by transferase CaiB. When gamma-butyrobetainyl-CoA is used as a cosubstrate, the first reaction is the CoA transfer. The optimal ratios of CaiB and CaiD during this hydration reaction, determined to be 4:1 when crotonobetainyl-CoA is used as cosubstrate and 5:1 when gamma-butyrobetainyl-CoA is used as cosubstrate, are different from that found for in vivo conditions, i.e. 1:3
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additional information
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enzyme CaiB acts as betainyl-CoA transferase specific for carnitine, crotonobetaine, gamma-butyrobetaine and its CoA derivatives. Transferase reaction proceeds, following a sequential bisubstrate mechanism. No substrates: CoA, acetoacetyl-CoA, acetyl-CoA, crotonyl-CoA, hydroxybutyryl-CoA, palmitoyl-CoA, succinyl-CoA
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additional information
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enzyme CaiB alone is unable to convert crotonobetaine into L-(-)-carnitine even in the presence of the cosubstrates crotonobetainyl-CoA or gamma-butyrobetainyl-CoA, which are essential for this biotransformation. The presence of both CaiB and CaiD protein and cosubstrate crotonobetainyl-CoA or gamma-butyrobetainyl-CoA are essential
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additional information
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enzyme CaiB acts as betainyl-CoA transferase specific for carnitine, crotonobetaine, gamma-butyrobetaine and its CoA derivatives. Transferase reaction proceeds, following a sequential bisubstrate mechanism. No substrates: CoA, acetoacetyl-CoA, acetyl-CoA, crotonyl-CoA, hydroxybutyryl-CoA, palmitoyl-CoA, succinyl-CoA
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additional information
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enzyme CaiB alone is unable to convert crotonobetaine into L-(-)-carnitine even in the presence of the cosubstrates crotonobetainyl-CoA or gamma-butyrobetainyl-CoA, which are essential for this biotransformation. The presence of both CaiB and CaiD protein and cosubstrate crotonobetainyl-CoA or gamma-butyrobetainyl-CoA are essential
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Engemann, C.; Elssner, T.; Pfeifer, S.; Krumbholz, C.; Maier, T.; Kleber, H.P.
Identification and functional characterisation of genes and corresponding enzymes involved in carnitine metabolism of Proteus sp.
Arch. Microbiol.
183
176-189
2005
Proteus sp. (Q8GB19), Proteus sp. LE138 (Q8GB19)
brenda
Stenmark, P.; Gurmu, D.; Nordlund, P.
Crystal structure of CaiB, a type-III CoA transferase in carnitine metabolism
Biochemistry
43
13996-14003
2004
Escherichia coli (P31572)
brenda
Engemann, C.; Elssner, T.; Kleber, H.P.
Biotransformation of crotonobetaine to L(-)-carnitine in Proteus sp.
Arch. Microbiol.
175
353-359
2001
Proteus sp. (Q8GB19), Proteus sp. LE138 (Q8GB19)
brenda
Elssner, T.; Engemann, C.; Baumgart, K.; Kleber, H.P.
Involvement of coenzyme A esters and two new enzymes, an enoyl-CoA hydratase and a CoA-transferase, in the hydration of crotonobetaine to L-carnitine by Escherichia coli
Biochemistry
40
11140-11148
2001
Escherichia coli (P31572), Escherichia coli
brenda
Rangarajan, E.S.; Li, Y.; Iannuzzi, P.; Cygler, M.; Matte, A.
Crystal structure of Escherichia coli crotonobetainyl-CoA: carnitine CoA-transferase (CaiB) and its complexes with CoA and carnitinyl-CoA
Biochemistry
44
5728-5738
2005
Escherichia coli (P31572), Escherichia coli
brenda
Sevilla, A.; Vera, J.; Diaz, Z.; Canovas, M.; Torres, N.V.; Iborra, J.L.
Design of metabolic engineering strategies for maximizing L-(-)-carnitine production by Escherichia coli. Integration of the metabolic and bioreactor levels
Biotechnol. Prog.
21
329-337
2005
Escherichia coli
brenda
Bernal, V.; Masdemont, B.; Arense, P.; Canovas, M.; Iborra, J.L.
Redirecting metabolic fluxes through cofactor engineering: Role of CoA-esters pool during L(-)-carnitine production by Escherichia coli
J. Biotechnol.
132
110-117
2007
Escherichia coli
brenda
2.8.3.21 L-carnitine CoA-transferase
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