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Saccharopine is an intermediate in the metabolism of amino acid lysine. It is a precursor of lysine in the alpha-aminoadipate pathway which occurs in a few lower fungi, the higher fungi, and euglenids. In mammals and higher plants saccharopine is an intermediate in the degradation of lysine, formed by condensation of lysine and alpha-ketoglutarate.

§Reaction

The reactions involved, catalysed by saccharopine dehydrogenases, are:

lysine + alpha-ketoglutarate ⇌ saccharopine ⇌ glutamate + 2-aminoadipate 6-semialdehyde

§Pathology

Saccharopinuria (high amounts of saccharopine in the urine) and saccharopinemia (an excess of saccharopine in the blood) are conditions present in some inherited disorders of lysine degradation.

§History

Saccharopine was first isolated in 1961 from yeasts (Saccharomyces, hence the name) by Darling and Larsen.^[2]

§See also

Opines

§References

^ "N-(5-AMINO-5-CARBOXYPENTYL)GLUTAMIC ACID - Compound Summary". PubChem Compound. USA: National Center for Biotechnology Information. 23 June 2005. Identification. Retrieved 11 July 2012.
^ Darling, S., and Larsen, P. O., Saccharopine, a new amino acid in Baker's and Brewer's yeast: I. Isolation and properties. Acta Chem. Scand., 15, 743 (1961).

English Journal

Pathways and substrate-specific regulation of amino acid degradation in Phaeobacter inhibens DSM 17395 (archetype of the marine Roseobacter clade).

Drüppel K, Hensler M, Trautwein K, Koßmehl S, Wöhlbrand L, Schmidt-Hohagen K, Ulbrich M, Bergen N, Meier-Kolthoff JP, Göker M, Klenk HP, Schomburg D, Rabus R.Author information Institute for Chemistry and Biology of the Marine Environment (ICBM), Carl von Ossietzky University Oldenburg, Oldenburg, Germany.AbstractCombining omics and enzymatic approaches, catabolic routes of nine selected amino acids (tryptophan, phenylalanine, methionine, leucine, isoleucine, valine, histidine, lysine and threonine) were elucidated in substrate-adapted cells of Phaeobacter inhibens DSM 17395 (displaying conspicuous morphotypes). The catabolic network [excluding tricarboxylic acid (TCA) cycle] was reconstructed from 71 genes (scattered across the chromosome; one-third newly assigned), with 69 encoded proteins and 20 specific metabolites identified, and activities of 10 different enzymes determined. For example, Ph. inhibens DSM 17395 does not degrade lysine via the widespread saccharopine pathway but might rather employ two parallel pathways via 5-aminopentanoate or 2-aminoadipate. Tryptophan degradation proceeds via kynurenine and 2-aminobenzoate; the latter is metabolized as known from Azoarcus evansii. Histidine degradation is analogous to the Pseudomonas-type Hut pathway via N-formyl-l-glutamate. For threonine, only one of the three genome-predicted degradation pathways (employing threonine 3-dehydrogenase) is used. Proteins of the individual peripheral degradation sequences in Ph. inhibens DSM 17395 were apparently substrate-specifically formed contrasting the non-modulated TCA cycle enzymes. Comparison of genes for the reconstructed amino acid degradation network in Ph. inhibens DSM 17395 across 27 other complete genomes of Roseobacter clade members revealed most of them to be widespread among roseobacters.
Environmental microbiology.Environ Microbiol.2014 Jan;16(1):218-38. doi: 10.1111/1462-2920.12276. Epub 2013 Oct 27.
Combining omics and enzymatic approaches, catabolic routes of nine selected amino acids (tryptophan, phenylalanine, methionine, leucine, isoleucine, valine, histidine, lysine and threonine) were elucidated in substrate-adapted cells of Phaeobacter inhibens DSM 17395 (displaying conspicuous morphotyp
PMID 24165547

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

Hallen A, Jamie JF, Cooper AJ.Author information Department of Chemistry and Biomolecular Sciences, Macquarie University, Balaclava Road, North Ryde, NSW, 2109, Australia, andre.hallen@mq.edu.au.AbstractThe 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 ∆(1)-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 ∆(1)-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 inter-relationship 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.
Amino acids.Amino Acids.2013 Dec;45(6):1249-72. doi: 10.1007/s00726-013-1590-1. Epub 2013 Sep 17.
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 �
PMID 24043460

Genome-wide analysis of lysine catabolism in bacteria reveals new connections with osmotic stress resistance.

Neshich IA, Kiyota E, Arruda P.Author information Centro de Biologia Molecular e Engenharia Genética, Universidade Estadual de Campinas (UNICAMP), Campinas, SP, Brazil.AbstractLysine is catabolized via the saccharopine pathway in plants and mammals. In this pathway, lysine is converted to α-aminoadipic-δ-semialdehyde (AASA) by lysine-ketoglutarate reductase/saccharopine dehydrogenase (LKR/SDH); thereafter, AASA is converted to aminoadipic acid (AAA) by α-aminoadipic-δ-semialdehyde dehydrogenase (AASADH). Here, we investigate the occurrence, genomic organization and functional role of lysine catabolic pathways among prokaryotes. Surprisingly, only 27 species of the 1478 analyzed contain the lkr and sdh genes, whereas 323 species contain aasadh orthologs. A sdh-related gene, identified in 159 organisms, was frequently found contiguously to an aasadh gene. This gene, annotated as lysine dehydrogenase (lysdh), encodes LYSDH an enzyme that directly converts lysine to AASA. Pipecolate oxidase (PIPOX) and lysine-6-aminotransferase (LAT), that converts lysine to AASA, were also found associated with aasadh. Interestingly, many lysdh-aasadh-containing organisms live under hyperosmotic stress. To test the role of the lysine-to-AASA pathways in the bacterial stress response, we subjected Silicibacter pomeroyi to salt stress. All but lkr, sdh, lysdh and aasadh were upregulated under salt stress conditions. In addition, lysine-supplemented culture medium increased the growth rate of S. pomeroyi under high-salt conditions and induced high-level expression of the lysdh-aasadh operon. Finally, transformation of Escherichia coli with the S. pomeroyi lysdh-aasadh operon resulted in increased salt tolerance. The transformed E. coli accumulated high levels of the compatible solute pipecolate, which may account for the salt resistance. These findings suggest that the lysine-to-AASA pathways identified in this work may have a broad evolutionary importance in osmotic stress resistance.
The ISME journal.ISME J.2013 Dec;7(12):2400-10. doi: 10.1038/ismej.2013.123. Epub 2013 Jul 25.
Lysine is catabolized via the saccharopine pathway in plants and mammals. In this pathway, lysine is converted to α-aminoadipic-δ-semialdehyde (AASA) by lysine-ketoglutarate reductase/saccharopine dehydrogenase (LKR/SDH); thereafter, AASA is converted to aminoadipic acid (AAA) by α-aminoadipic-δ
PMID 23887172

Japanese Journal

Characterization of Two Fructosyl-Amino Acid Oxidase Homologs of Schizosaccharomyces pombe (ENZYMOLOGY, PROTEIN ENGINEERING, AND ENZYME TECHNOLOGY)

Yoshida Nobuyuki,Akazawa Shin-ichi,Katsuragi Tohoru [他],TANI YOSHIKI
Journal of bioscience and bioengineering 97(4), 278-280, 2004-04-25
… It was suggested that Fap1 and Fap2 are an L-pipecolic acid oxidase and L-saccharopine oxidase, respectively. …
NAID 110002665297

Novel chimeric spermidine synthase-saccharopine dehydrogenase gene (SPE3-LYS9) in the human pathogen Cryptococcus neoformans

KINGSBURY J. M.
Eukaryot. Cell 3, 752-763, 2004
NAID 30002293717

622 分裂酵母に見いだされたフルクトシルアミノ酸オキシダーゼホモログ遺伝子の解析(酵素・酵素工学・タンパク質工学,一般講演)

赤澤真一,吉田信行,桂樹徹,谷吉樹
日本生物工学会大会講演要旨集平成14年度, 100, 2002-09-25
NAID 110007320447

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★リンクテーブル★

リンク元	「サッカロピン」
拡張検索	「saccharopine dehydrogenase」

「サッカロピン」

Saccharopine
Names
	IUPAC name 2-[(5-Amino-5-carboxypentyl)amino]pentanedioic acid
Identifiers
3DMet	B01246
CAS Registry Number	997-68-2
ChEBI	CHEBI:16927
ChemSpider	141086
DrugBank	DB04207
	InChI InChI=1S/C11H20N2O6/c12-7(10(16)17)3-1-2-6-13-8(11(18)19)4-5-9(14)15/h7-8,13H,1-6,12H2,(H,14,15)(H,16,17)(H,18,19) ; Key: ZDGJAHTZVHVLOT-UHFFFAOYSA-N ;
Jmol-3D images	Image; Image
KEGG	C00449
MeSH	saccharopine
PubChem	160556
	SMILES NC(CCCCNC(CCc(:[o]):[oH])c(:[o]):[oH])c(:[o]):[oH] ; NC(CCCCNC(CCC(O)=O)C(O)=O)C(O)=O ;
Properties
Molecular formula	C11H20N2O6
Molar mass	276.29 g·mol−1
Related compounds
Related alkanoic acids	4-(γ-Glutamylamino)butanoic acid; Hypusine;
Related compounds	Palmitoylethanolamide
	Except where noted otherwise, data is given for materials in their standard state (at 25 °C (77 °F), 100 kPa)
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	Infobox references