The Preparation and Some Properties of α-Aminoadipic-δ-Semialdehyde (Δ<sup>1</sup>-Piperideine-6-carboxylic Acid)<sup>*</sup>

Aspen, Anita J.; Meister, Alton

doi:10.1021/bi00910a009

Cited by 32 publications

(4 citation statements)

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“…Δ 1 -Piperideine-2-carboxylate formed from the spontaneous cyclization of KAC is reduced to l -pipecolate by specific reductases (Meister 1962; Meister and Buckley 1957; Aspen and Meister 1962a, b; Meister et al 1957). Meister (1962), Meister and Buckley (1957) and Meister et al (1957) partially purified an imine reductase from rat kidney and were the first to show that mammalian tissues contain reductase(s) that reduce the imine double bond of P2C and also that of its five-membered ring analog [i.e., Δ 1 -pyrroline-2-carboxylate (Pyr2C)], forming only the l -enantiomers of pipecolate and proline, respectively.…”

Section: The Discovery Of Specific Cytosolic P2c Reductasesmentioning

confidence: 99%

Lysine metabolism in mammalian brain: an update on the importance of recent discoveries

2013

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The lysine catabolism pathway differs in adult mammalian brain from that in extracerebral tissues. The saccharopine pathway is the predominant lysine degradative pathway in extracerebral tissues, whereas the pipecolate pathway predominates in adult brain. The two pathways converge at the level of Δ1-piperideine-6-carboxylate (P6C), which is in equilibrium with its open-chain aldehyde form, namely, α-aminoadipate δ-semialdehyde (AAS). A unique feature of the pipecolate pathway is the formation of the cyclic ketimine intermediate Δ1-piperideine-2-carboxylate (P2C) and its reduced metabolite l-pipecolate. A cerebral ketimine reductase (KR) has recently been identified that catalyzes the reduction of P2C to l-pipecolate. The discovery that this KR, which is capable of reducing not only P2C but also other cyclic imines, is identical to a previously well-described thyroid hormone-binding protein [μ-crystallin (CRYM)], may hold the key to understanding the biological relevance of the pipecolate pathway and its importance in the brain. The finding that the KR activity of CRYM is strongly inhibited by the thyroid hormone 3,5,3′-triiodothyronine (T3) has far-reaching biomedical and clinical implications. The interrelationship between tryptophan and lysine catabolic pathways is discussed in the context of shared degradative enzymes and also potential regulation by thyroid hormones. This review traces the discoveries of enzymes involved in lysine metabolism in mammalian brain. However, there still remain unanswered questions as regards the importance of the pipecolate pathway in normal or diseased brain, including the nature of the first step in the pathway and the relationship of the pipecolate pathway to the tryptophan degradation pathway.

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Section: The Discovery Of Specific Cytosolic P2c Reductasesmentioning

confidence: 99%

Lysine metabolism in mammalian brain: an update on the importance of recent discoveries

2013

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“…5). One of the intermediates in this pathway, ␣-amino adipic semialdehyde, spontaneously cyclizes to P6C (46), which upon reduction yields pipecolate (Fig. 5).…”

Section: Discussionmentioning

confidence: 99%

Characterization and Metabolic Function of a Peroxisomal Sarcosine and Pipecolate Oxidase from Arabidopsis

Goyer

Johnson

Olsen

et al. 2004

Journal of Biological Chemistry

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Sarcosine oxidase (SOX) is known as a peroxisomal enzyme in mammals and as a sarcosine-inducible enzyme in soil bacteria. Its presence in plants was unsuspected until the Arabidopsis genome was found to encode a protein (AtSOX) with ϳ33% sequence identity to mammalian and bacterial SOXs. When overexpressed in Escherichia coli, AtSOX enhanced growth on sarcosine as sole nitrogen source, showing that it has SOX activity in vivo, and the recombinant protein catalyzed the oxidation of sarcosine to glycine, formaldehyde, and H 2 O 2 in vitro. AtSOX also attacked other N-methyl amino acids and, like mammalian SOXs, catalyzed the oxidation of L-pipecolate to ⌬ 1 -piperideine-6-carboxylate. Like bacterial monomeric SOXs, AtSOX was active as a monomer, contained FAD covalently bound to a cysteine residue near the C terminus, and was not stimulated by tetrahydrofolate. Although AtSOX lacks a typical peroxisome-targeting signal, in vitro assays established that it is imported into peroxisomes. Quantitation of mRNA showed that AtSOX is expressed at a low level throughout the plant and is not sarcosine-inducible. Consistent with a low level of AtSOX expression, Arabidopsis plantlets slowly metabolized supplied [ 14 C]sarcosine to glycine and serine. Gas chromatography-mass spectrometry analysis revealed low levels of pipecolate but almost no sarcosine in wild type Arabidopsis and showed that pipecolate but not sarcosine accumulated 6-fold when AtSOX expression was suppressed by RNA interference. Moreover, the pipecolate catabolite ␣-aminoadipate decreased 30-fold in RNA interference plants. These data indicate that pipecolate is the endogenous substrate for SOX in plants and that plants can utilize exogenous sarcosine opportunistically, sarcosine being a common soil metabolite.

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“…No color developed when the chromatograms were heated for 10-15 minutes at temperatures less them 60°. Pipecolic acid reacts relatively slowly with ninhydrin on paper chromatograms as compared to most of the -amino acids, and indeed the compound was readily identified as pipecolic acid by paper chromatography in four solvent systems (Aspen and Meister, 1962).…”

Section: Methodsmentioning

confidence: 99%

“…-Ketoe-aminocaproic acid (Meister, 1954) , aketo -Nacetyleaminocaproic acid (Meister, 1952), -ketoadipic acid (Gault, 1912), a-aminoadipic-5-semialdehyde and the TV-acetyl derivative of this compound (Aspen and Meister, 1962), piperidone carboxylic acid (Greenstein et al, 1953), and o-aminobenzaldehyde (Smith and Opie, 1955) were prepared as described. D-Amino acid oxidase was isolated from hog kidney according to Negelein and Bromel (1939).…”

Section: Methodsmentioning

confidence: 99%

Conversion of α-Aminoadipic Acid to L-Pipecolic Acid by Aspergillus nidulans^*

Aspen¹,

Meister²

1962

Biochemistry

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Two mutants of Aspergillus nidulans, which exhibit a growth response to L-lysine, but not to L--amincadipic acid, accumulated L-pipecolic acid when grown in media containing growth-limiting concentrations of L-lysine. No accumulation occurred when these mutants were grown on optimal concentrations of L-lysine, nor was pipecolic acid accumulation observed with other types of lysine-requiring mutants of A. nidulans. L-Pipecolic acid accumulation, but not growth, was delayed by addition of o-aminobenzaldehyde to the medium. Catalytic hydrogenation of extracts of cells grown in the presence of o-aminobenzaldehyde gave DL-pipecolic acid, whereas catalytic hydrogenation of da-aminoadipic-S-semialdehyde after prolonged treatment with o-aminobenzaldehyde gave D-pipecolic acid. The findings are consistent with the accumulation of Lpiperideine^-carboxylic acid in the presence of o-aminobenzaldehyde. Studies with C14-and N "-labeled -aminoadipic acid and C14-lysine indicate that the carbon chain of -aminoadipic acid rather than that of lysine is the major precursor of pipecolic acid, and that the nitrogen atom of -aminoadipic acid becomes the nitrogen atom of pipecolic acid.The participation of -aminoadipic acid in lysine biosynthesis in certain yeasts and fungi is suggested by the observation that several mutant microorganisms are able to utilize either lysine or -aminoadipic acid for growth (Mitchell and Houlahan, 1948;Bergstrom and Rottenberg, 1950), and by tracer studies on such a mutant of Neurospora crassa, which showed that C1 ^aminoadipic acid was converted to C1 '-lysine without significant change in specific radioactivity (Windsor, 1951). Although there is evidence that certain microorganisms can convert a-aminoadipic acid to lysine, the enzymatic reactions involved are not yet understood. A number of plausible intermediates may be considered, including aketoe-aminocaproic acid ( '-piperideine-2-carboxylic acid), a-aminoadipic-ó-semialdehyde ( 1piperideine-6-car boxy lie acid), and pipecolic acid; the possibility that iV-acyl derivatives of these compounds and of lysine may be involved must also be considered.In the course of studies on the biosynthesis of * The authors acknowledge the generous support of the

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The Preparation and Some Properties of α-Aminoadipic-δ-Semialdehyde (Δ¹-Piperideine-6-carboxylic Acid)^*

Cited by 32 publications

References 24 publications

Lysine metabolism in mammalian brain: an update on the importance of recent discoveries

Lysine metabolism in mammalian brain: an update on the importance of recent discoveries

Characterization and Metabolic Function of a Peroxisomal Sarcosine and Pipecolate Oxidase from Arabidopsis

Conversion of α-Aminoadipic Acid to L-Pipecolic Acid by Aspergillus nidulans^*

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The Preparation and Some Properties of α-Aminoadipic-δ-Semialdehyde (Δ1-Piperideine-6-carboxylic Acid)*

Cited by 32 publications

References 24 publications

Lysine metabolism in mammalian brain: an update on the importance of recent discoveries

Lysine metabolism in mammalian brain: an update on the importance of recent discoveries

Characterization and Metabolic Function of a Peroxisomal Sarcosine and Pipecolate Oxidase from Arabidopsis

Conversion of α-Aminoadipic Acid to L-Pipecolic Acid by Aspergillus nidulans*

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The Preparation and Some Properties of α-Aminoadipic-δ-Semialdehyde (Δ¹-Piperideine-6-carboxylic Acid)^*

Conversion of α-Aminoadipic Acid to L-Pipecolic Acid by Aspergillus nidulans^*