α-Ketoglutarate and hydroxylation of γ-butyrobetaine

Lindstedt, Göran; Lindstedt, Sven; Olander, Birgit; Tofft, Marianne

doi:10.1016/0304-4165(68)90317-6

Cited by 43 publications

(14 citation statements)

References 11 publications

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“…The synthesis of hydroxylysine was accompanied by the decarboxylation of a-ketoglutarate. The results therefore established protocollagen lysine hydroxylase as the fourth hydroxylase which decarboxylates a-ketoglutarate in the course of substrate hydroxylation (Lindstedt et a/., 1968;Rhoads and Udenfriend, 1968;McCroskey et d., 1971). Succinate and carbon dioxide were shown to be products of the reaction and the amount of carbon dioxide released was equimolar with the amount of hydroxylysine synthesized.…”

Section: Discussionmentioning

confidence: 88%

Protocollagen lysine hydroxylase. Hydroxylation of synthetic peptides and the stoichiometric decarboxylation of α-ketoglutarate

Kivirikko¹,

K²,

Sakakibara³

et al. 1972

Biochemistry

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A series of synthetic peptides was prepared and used to study protocollagen lysine hydroxylase, the enzyme which synthesizes the hydroxylysine in collagen. The enzyme was purified 150-to 250-fold from chick embryo extracts and it was completely free of protocollagen proline hydroxylase activity. Several synthetic peptides competitively prevented the hydroxylation of lysine-labeled [ 14C]protocollagen by protocollagen lysine hydroxylase. When the peptides were examined directly as substrates for the enzyme, the synthesis of measurable amounts of hydroxylysine was observed for the first time. The synthesis of hydroxylysine was accompanied by the conversion of a-ketoglutarate to C02 and succinate, indicating that the enzyme belongs to the new class of oxygenases which decarboxylate a-ketoglutarate during substrate hydroxylation. The release of [14C]COr from [l-14Cl]a-ketoglutarate was equimolar with the synthesis of hydroxylysine and therefore the amount of ['CC]CO2 released could be used as a simple assay for the enzymic reaction. Three peptides were synthesized which had amino acid sequences comparable to amino acid sequences around glycosylated hydroxylysine in collagen. The peptide "L-I" had the sequence Ala-Arg-Gly-Ile-Lys-Gly-Ile-Arg-GlyPhe-Ser-Gly, "L-11" the sequence Ala-Arg-Gly-Met-Lys-GlyHis-Arg-Gly-(Pro-Pro-Gly),, and "L-111" the sequence (ProPro-Gly),-Ala-Arg-Gly-Met-Lys-Gly-His-Arg -Gly -(Prn -Pro-

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Section: Discussionmentioning

confidence: 88%

Protocollagen lysine hydroxylase. Hydroxylation of synthetic peptides and the stoichiometric decarboxylation of α-ketoglutarate

Kivirikko¹,

K²,

Sakakibara³

et al. 1972

Biochemistry

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“…BBD catalyses the stereospecific hydroxylation of butyrobetaine to -carnitine [47]. Lindstedt and colleagues [48][49][50] were the first to partially purify a BBD from Pseudomonas sp. AK 1, a bacterial strain that can grow on butyrobetaine as the sole source of carbon and nitrogen.…”

Section: Bbdmentioning

confidence: 99%

Carnitine biosynthesis in mammals

Vaz¹,

Wanders²

2002

Biochem. J.

449

384

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Carnitine is indispensable for energy metabolism, since it enables activated fatty acids to enter the mitochondria, where they are broken down via beta-oxidation. Carnitine is probably present in all animal species, and in numerous micro-organisms and plants. In mammals, carnitine homoeostasis is maintained by endogenous synthesis, absorption from dietary sources and efficient tubular reabsorption by the kidney. This review aims to cover the current knowledge of the enzymological, molecular, metabolic and regulatory aspects of mammalian carnitine biosynthesis, with an emphasis on the human and rat.

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“…AK1 (Lindstedt et al, 1970a, b; Rüetschi et al, 1993) and Pseudomonas sp. L1 (Lu et al, 2012), and both enzymes are homologous to the animal c-butyrobetaine hydroxylase in their requirement for oxygen and the cofactors iron, ascorbate, and a-ketogluterate (Lindstedt & Lindstedt, 1970;Lindstedt et al, 1968). …”

mentioning

confidence: 99%

Carnitine in bacterial physiology and metabolism

2015

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Carnitine is a quaternary amine compound found at high concentration in animal tissues, particularly muscle, and is most well studied for its contribution to fatty acid transport into mitochondria. In bacteria, carnitine is an important osmoprotectant, and can also enhance thermotolerance, cryotolerance and barotolerance. Carnitine can be transported into the cell or acquired from metabolic precursors, where it can serve directly as a compatible solute for stress protection or be metabolized through one of a few distinct pathways as a nutrient source. In this review, we summarize what is known about carnitine physiology and metabolism in bacteria. In particular, recent advances in the aerobic and anaerobic metabolic pathways as well as the use of carnitine as an electron acceptor have addressed some long-standing questions in the field. Received 5 January 2015 Accepted 17 March 2015Introduction Carnitine (c-trimethylamino-b-hydroxybutyric acid) ( Fig. 1) is a quaternary amine compound that can be produced by all domains of life, and was discovered in muscle extract in 1905 by Gulewitsch & Krimberg (1905) and Kutscher (1905). It was shown to be essential for larval development of the mealworm Tenebrio molitor and was originally designated vitamin B T based on this requirement. Later, it was discovered that carnitine can be synthesized in mammals and is now considered to be a quasi-nutrient or conditionally essential nutrient (Flanagan et al., 2010), as neonates have reduced biosynthesis and rely on placental transfer of carnitine in utero and exogenous sources after birth (Combs, 2012). Fifty years after the discovery of carnitine, it was demonstrated that assorted Gram-positive and Gram-negative bacteria could use carnitine in either aerobic or anaerobic environments for a variety of cellular functions, including as an electron acceptor, as a compatible solute to survive environmental insults or as a sole carbon, nitrogen and energy source. Bacterial carnitine metabolism was most recently reviewed in 1998 (Bieber, 1988;Bremer, 1983;Kleber, 1997;Rebouche & Seim, 1998) and the field has seen important advances. This review summarizes what we knew at the time of the previous reviews and emphasizes what we have learned since, including: (i) how anaerobic bacteria synthesize and utilize crotonobetaine and carnitine as final electron acceptors, (ii) the impact of carnitine degradation by the intestinal microbiota and the genes responsible for this anaerobic conversion, (iii) the genes involved in aerobic degradation of carnitine, and (iv) how carnitine as a compatible solute impacts survival within and outside of the host. Carnitine in the environmentRecent work makes it clear that while animals represent the most readily accessible source of carnitine, carnitine is often present and sometimes abundant in soil and natural waters. Quaternary ammonium compounds are abundant in a number of soil ecosystems, including comprising a quarter of the most abundant organic nitrogen compounds in the soil water of a subalpine gras...

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α-Ketoglutarate and hydroxylation of γ-butyrobetaine

Cited by 43 publications

References 11 publications

Protocollagen lysine hydroxylase. Hydroxylation of synthetic peptides and the stoichiometric decarboxylation of α-ketoglutarate

Protocollagen lysine hydroxylase. Hydroxylation of synthetic peptides and the stoichiometric decarboxylation of α-ketoglutarate

Carnitine biosynthesis in mammals

Carnitine in bacterial physiology and metabolism

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