Formation of xylulose-5-phosphate (Homo sapiens)

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Bibliography

1. Maret W, Auld DS.; ''Purification and characterization of human liver sorbitol dehydrogenase.''; PubMed Europe PMC Scholia
2. Bunker RD, Bulloch EM, Dickson JM, Loomes KM, Baker EN.; ''Structure and function of human xylulokinase, an enzyme with important roles in carbohydrate metabolism.''; PubMed Europe PMC Scholia
3. Alvarez A, Martínez A, Ibarra B, Medina C, Bracamontes M, Perea J, Vaca G.; ''Membrane-bound sorbitol dehydrogenase in human red blood cells. Studies in normal subjects and in enzyme-deficient subjects with congenital cataracts.''; PubMed Europe PMC Scholia
4. Barski OA, Gabbay KH, Grimshaw CE, Bohren KM.; ''Mechanism of human aldehyde reductase: characterization of the active site pocket.''; PubMed Europe PMC Scholia
5. Nakagawa J, Ishikura S, Asami J, Isaji T, Usami N, Hara A, Sakurai T, Tsuritani K, Oda K, Takahashi M, Yoshimoto M, Otsuka N, Kitamura K.; ''Molecular characterization of mammalian dicarbonyl/L-xylulose reductase and its localization in kidney.''; PubMed Europe PMC Scholia
6. Wamelink MM, Struys EA, Jakobs C.; ''The biochemistry, metabolism and inherited defects of the pentose phosphate pathway: a review.''; PubMed Europe PMC Scholia
7. WINKELMAN J, ASHWELL G.; ''Enzymic formation of L-xylulose from beeta-keto-L-gulonic acid.''; PubMed Europe PMC Scholia
8. Karlsson C, Maret W, Auld DS, Höög JO, Jörnvall H.; ''Variability within mammalian sorbitol dehydrogenases. The primary structure of the human liver enzyme.''; PubMed Europe PMC Scholia
9. Pauly TA, Ekstrom JL, Beebe DA, Chrunyk B, Cunningham D, Griffor M, Kamath A, Lee SE, Madura R, Mcguire D, Subashi T, Wasilko D, Watts P, Mylari BL, Oates PJ, Adams PD, Rath VL.; ''X-ray crystallographic and kinetic studies of human sorbitol dehydrogenase.''; PubMed Europe PMC Scholia
10. El-Kabbani O, Ishikura S, Darmanin C, Carbone V, Chung RP, Usami N, Hara A.; ''Crystal structure of human L-xylulose reductase holoenzyme: probing the role of Asn107 with site-directed mutagenesis.''; PubMed Europe PMC Scholia
11. Ishikura S, Usami N, Araki M, Hara A.; ''Structural and functional characterization of rabbit and human L-gulonate 3-dehydrogenase.''; PubMed Europe PMC Scholia
12. Boué F, Blais J, Sullivan R.; ''Surface localization of P34H an epididymal protein, during maturation, capacitation, and acrosome reaction of human spermatozoa.''; PubMed Europe PMC Scholia
13. Wang YM, Van Eys J.; ''The enzymatic defect in essential pentosuria.''; PubMed Europe PMC Scholia
14. Pierce SB, Spurrell CH, Mandell JB, Lee MK, Zeligson S, Bereman MS, Stray SM, Fokstuen S, MacCoss MJ, Levy-Lahad E, King MC, Motulsky AG.; ''Garrod's fourth inborn error of metabolism solved by the identification of mutations causing pentosuria.''; PubMed Europe PMC Scholia

History

External references

DataNodes

Name	Type	Database reference	Comment
3-dehydro-L-gulonate	Metabolite	CHEBI:57655 (ChEBI)
ADP	Metabolite	CHEBI:456216 (ChEBI)
AKR1A1	Protein	P14550 (Uniprot-TrEMBL)
ATP	Metabolite	CHEBI:30616 (ChEBI)
CO2	Metabolite	CHEBI:16526 (ChEBI)
CRYL1	Protein	Q9Y2S2 (Uniprot-TrEMBL)
CRYL1 dimer	Complex	R-HSA-5661289 (Reactome)
D-glucuronate	Metabolite	CHEBI:15748 (ChEBI)
D-xylulose	Metabolite	CHEBI:17140 (ChEBI)
DCXR	Protein	Q7Z4W1 (Uniprot-TrEMBL)
DCXR tetramer	Complex	R-HSA-5660027 (Reactome)
H+	Metabolite	CHEBI:15378 (ChEBI)
KGPDC		R-HSA-5661266 (Reactome)
L-gulonate	Metabolite	CHEBI:13115 (ChEBI)
L-xylulose	Metabolite	CHEBI:17399 (ChEBI)
NAD+	Metabolite	CHEBI:57540 (ChEBI)
NADH	Metabolite	CHEBI:57945 (ChEBI)
NADP+	Metabolite	CHEBI:18009 (ChEBI)
NADPH	Metabolite	CHEBI:16474 (ChEBI)
SORD	Protein	Q00796 (Uniprot-TrEMBL)
SORD tetramer	Complex	R-HSA-5652211 (Reactome)
XY5P	Metabolite	CHEBI:57737 (ChEBI)
XYLB	Protein	O75191 (Uniprot-TrEMBL)
Zn2+	Metabolite	CHEBI:29105 (ChEBI)
xylitol	Metabolite	CHEBI:17151 (ChEBI)

Annotated Interactions

Source	Target	Type	Database reference	Comment
	3-dehydro-L-gulonate	Arrow	R-HSA-5661290 (Reactome)
3-dehydro-L-gulonate			R-HSA-5662473 (Reactome)
	ADP	Arrow	R-HSA-5662466 (Reactome)
AKR1A1		mim-catalysis	R-HSA-5661256 (Reactome)
ATP			R-HSA-5662466 (Reactome)
	CO2	Arrow	R-HSA-5662473 (Reactome)
CRYL1 dimer		mim-catalysis	R-HSA-5661290 (Reactome)
D-glucuronate			R-HSA-5661256 (Reactome)
	D-xylulose	Arrow	R-HSA-5662471 (Reactome)
D-xylulose			R-HSA-5662466 (Reactome)
DCXR tetramer		mim-catalysis	R-HSA-5661240 (Reactome)
	H+	Arrow	R-HSA-5661290 (Reactome)
	H+	Arrow	R-HSA-5662471 (Reactome)
H+			R-HSA-5661240 (Reactome)
H+			R-HSA-5661256 (Reactome)
KGPDC		mim-catalysis	R-HSA-5662473 (Reactome)
	L-gulonate	Arrow	R-HSA-5661256 (Reactome)
L-gulonate			R-HSA-5661290 (Reactome)
	L-xylulose	Arrow	R-HSA-5662473 (Reactome)
L-xylulose			R-HSA-5661240 (Reactome)
NAD+			R-HSA-5661290 (Reactome)
NAD+			R-HSA-5662471 (Reactome)
	NADH	Arrow	R-HSA-5661290 (Reactome)
	NADH	Arrow	R-HSA-5662471 (Reactome)
	NADP+	Arrow	R-HSA-5661240 (Reactome)
	NADP+	Arrow	R-HSA-5661256 (Reactome)
NADPH			R-HSA-5661240 (Reactome)
NADPH			R-HSA-5661256 (Reactome)
			R-HSA-5661240 (Reactome)	L-xylulose reductase (DCXR, also known as dicarbonyl/L-xylulose reductase) catalyzes the reversible NADPH dependent reduction of cytosolic L-xylulose to xylitol (Nakagawa et al. 2002). The enzyme is a tetramer (El Kabbani et al.2004) and may be associated with the plasma membrane (Boue et al. 1996). Mutations that inactivate DCXR are associated with essential pentosuria (Pierce et al. 2011; Wang & van Eys 1970).
			R-HSA-5661256 (Reactome)	Cytosolic AKR1A1 (Aldo-keto reductase family 1 member A1) catalyzes the reduction by NADPH of D-glucuronate to L-gulonate (Barski et al. 1995).
			R-HSA-5661290 (Reactome)	Cytosolic CRYL1 (lambda-crystallin homolog, also known as L-gulonate 3-dehydrogenase) dimer catalyzes the NAD-dependent dehydrogenation of L-gulonate to form 3-dehydro-L-gulonate. The CRYL1 protein also functions as a lens crystallin, hence its name (Ishikura et al. 2005).
			R-HSA-5662466 (Reactome)	Cytosolic xylulose kinase (XYLB) catalyzes the phosphorylation of D-xylulose to form D-xylulose-5-phosphate (XY5P) (Bunker et al. 2013).
			R-HSA-5662471 (Reactome)	Tetrameric sorbitol dehydrogenase (SORD tetramer) catalyzes the NAD-dependent oxidation of xylitol to form D-xylulose (Alvarez et al. 1993; Karlsson et al. 1989; Maret & Auld 1988; Pauly et al. 2003).
			R-HSA-5662473 (Reactome)	Cytosolic dehydro-L-gulonate decarboxylase (KGPDC) catalyzes the conversion of 3-dehydro-L-gulonate to L-xylulose and CO2. Studies in vivo provide indirect but strong evidence that this reaction occurs in humans and guinea pigs and dehydro-L-gulonate decarboxylase enzyme has been partially purified from guinea pigs (Winkelman & Ashwell 1961). Its amino acid sequence is unknown, however.
SORD tetramer		mim-catalysis	R-HSA-5662471 (Reactome)
	XY5P	Arrow	R-HSA-5662466 (Reactome)
XYLB		mim-catalysis	R-HSA-5662466 (Reactome)
	xylitol	Arrow	R-HSA-5661240 (Reactome)
xylitol			R-HSA-5662471 (Reactome)