Uncoupling in the γ-butyrobetaine hydroxylase reaction by D=- and L=-carnitine

Holme, Elisabeth; Lindstedt, Sven; Nordin, Ingalill

doi:10.1016/0006-291x(82)91522-4

Cited by 31 publications

(28 citation statements)

References 14 publications

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“…2 and Tables I and II). While it is known that prime substrate oxidation is not always fully coupled to that of 2OG 7 (4,(55)(56)(57)(58), the results support previous work implying that both ANS and FLS possess a broad substrate selectivity in vitro (21,26,28,29,49) and provide some new insights.…”

Section: The Effect Of Different Flavonoid Substrates On the Rate Of supporting

confidence: 86%

Mechanistic Studies on Three 2-Oxoglutarate-dependent Oxygenases of Flavonoid Biosynthesis

Turnbull¹,

Nakajima

Welford³

et al. 2004

Journal of Biological Chemistry

188

154

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Anthocyanidin synthase (ANS), flavonol synthase (FLS), and flavanone 3␤-hydroxylase (FHT) are involved in the biosynthesis of flavonoids in plants and are all members of the family of 2-oxoglutarate-and ferrous iron-dependent oxygenases. ANS, FLS, and FHT are closely related by sequence and catalyze oxidation of the flavonoid "C ring"; they have been shown to have overlapping substrate and product selectivities. In the initial steps of catalysis, 2-oxoglutarate and dioxygen are thought to react at the ferrous iron center producing succinate, carbon dioxide, and a reactive ferryl intermediate, the latter of which can then affect oxidation of the flavonoid substrate.

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Section: The Effect Of Different Flavonoid Substrates On the Rate Of supporting

confidence: 86%

Mechanistic Studies on Three 2-Oxoglutarate-dependent Oxygenases of Flavonoid Biosynthesis

Turnbull¹,

Nakajima

Welford³

et al. 2004

Journal of Biological Chemistry

188

154

View full text Add to dashboard Cite

show abstract

“…It has been shown that the enzyme is indeed a dioxygenase by means of asO 2 labeling [116] and the hydroxylation has been found to proceed with retention of configuration C-3 [117]. Furthermore, there is an uncoupling of ~-oxoglutarate decarboxylation from y-butyrobetaine hydroxylase [118].…”

Section: L-carnitine Synthesis From Y-butyrobetainementioning

confidence: 93%

Synthesis of l-carnitine by microorganisms and isolated enzymes

Jung

Kleber

1993

Measurement and Control

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“…Furthermore, the modified EGF, which has the required amino acid sequence (residues 3-5), did not stimulate the 2-oxoglutarate decarboxylation. Uncoupling (i.e., decarboxylation of 2-oxoglutarate without concomitant hydroxylation) has been demonstrated in reactions catalyzed by proline (31), y-butyrobetaine (32,33), and thymine (34,35) hydroxylases in the presence of substrate analogues. With the natural substrates, however, there is a close coupling between proline (14) and lysine hydroxylation (36) and 2-oxoglutarate decarboxylation.…”

Section: Discussionmentioning

confidence: 99%

Hydroxylation of aspartic acid in domains homologous to the epidermal growth factor precursor is catalyzed by a 2-oxoglutarate-dependent dioxygenase.

Stenflo

Holme

Lindstedt

et al. 1989

Proc. Natl. Acad. Sci. U.S.A.

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ABSTRACT3-Hydroxyaspartic acid and 3-hydroxyasparagine are two rare amino acids that are present in domains homologous to the epidermal growth factor precursor in vitamin K-dependent plasma proteins as well as in proteins that do not require vitamin K for normal biosynthesis. They are formed by posttranslational hydroxylation of aspartic acid and asparagine, respectively. The first epidermal growth factorlike domain in factor IX (residues 45-87) was synthesized with aspartic acid in position 64, replacing 3-hydroxyaspartic acid. It was used as substrate in a hydroxylase assay with rat liver microsomes as the source of enzyme and reaction conditions that satisfy the requirements of 2-oxoglutarate-dependent dioxygenases. The synthetic peptide stimulated the 2-oxoglutarate decarboxylation in contrast to synthetic, modified epidermal growth factor (Met-21 and His-22 deleted and Glu-24 replaced by Asp) and synthetic peptides corresponding to residues 60-71 in human factor IX. This indicates that the hydroxylase is a 2-oxoglutarate-dependent dioxygenase with a selective substrate requirement.

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Uncoupling in the γ-butyrobetaine hydroxylase reaction by D=- and L=-carnitine

Cited by 31 publications

References 14 publications

Mechanistic Studies on Three 2-Oxoglutarate-dependent Oxygenases of Flavonoid Biosynthesis

Mechanistic Studies on Three 2-Oxoglutarate-dependent Oxygenases of Flavonoid Biosynthesis

Synthesis of l-carnitine by microorganisms and isolated enzymes

Hydroxylation of aspartic acid in domains homologous to the epidermal growth factor precursor is catalyzed by a 2-oxoglutarate-dependent dioxygenase.

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