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Information on EC 3.2.1.62 - glycosylceramidase and Organism(s) Homo sapiens and UniProt Accession P09848
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3.2.1.62 glycosylceramidaseIUBMB Comments
The enzyme, found in the intestinal mucosa, hydrolyses beta-D-glucosyl and beta-D-galactosyl residues from a very broad range of substrates using a retaining mechanism. Characterized substrates include glucosyl- and galactosyl-ceramides , O3-, O4'- and O7-glucosylated flavonoids , and the 2'-O-glucosylated dihydrochalcone phlorizin . The enzyme includes two glycosyl hydrolase domains, both belonging to the GH1 family. While one domain is responsible for the activity described here, the other catalyses the reaction of EC 3.2.1.108, lactase [4,5]. cf. EC 3.2.1.45, glucosylceramidase and EC 3.2.1.46, galactosylceramidase.
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Word Map
- 3.2.1.62
- lactose
- sucrase-isomaltase
- enterocytes
-
brush
- jejunum
-
pro-lph
- microvillus
-
brush-border
- sucrase
- hypolactasia
- disaccharidase
-
adult-type
- maltase-glucoamylase
-
enterocyte-specific
-
mannose-rich
-
beta-glycosidase
-
transport-competent
-
3.4.11.7
- medicine
-
non-persistence
-
crypt-villus
The taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Reaction Schemes
a beta-D-galactosyl-N-acylsphingosine
+
=
+
a flavonoid-O-beta-D-glucoside
+
=
+
Synonyms
lactase-phlorizin hydrolase, phlorizin hydrolase, cerebrosidase, endoglycoceramidase ii, egcrp1, glycosylceramidase, egcii, endoglycoceramidase-related protein 1, phloretin-glucosidase, endo-glycoceramidase ii, 
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topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
cerebrosidase
-
-
-
-
glycosyl ceramide glycosylhydrolase
-
-
-
-
lactase-phlorizin hydrolase
LCT
-
-
-
-
LPH
phloretin-glucosidase
-
-
-
-
phloridzin glucosidase
-
-
-
-
phlorizin beta-glucosidase
-
-
-
-
phlorizin hydrolase
-
-
-
-
lactase-phlorizin hydrolase
-
-
-
-
lactase-phlorizin hydrolase
-
brush border membrane (BBM)-associated enzyme in intestinal cells
LPH
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of O-glycosyl bond
hydrolysis of O-glycosyl bond
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
beta-D-glucosyl-N-acylsphingosine glycohydrolase (configuration-retaining)
The enzyme, found in the intestinal mucosa, hydrolyses beta-D-glucosyl and beta-D-galactosyl residues from a very broad range of substrates using a retaining mechanism. Characterized substrates include glucosyl- and galactosyl-ceramides [3], O3-, O4'- and O7-glucosylated flavonoids [6], and the 2'-O-glucosylated dihydrochalcone phlorizin [1]. The enzyme includes two glycosyl hydrolase domains, both belonging to the GH1 family. While one domain is responsible for the activity described here, the other catalyses the reaction of EC 3.2.1.108, lactase [4,5]. cf. EC 3.2.1.45, glucosylceramidase and EC 3.2.1.46, galactosylceramidase.
CAS REGISTRY NUMBER
COMMENTARY
9033-10-7
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
4-methylumbelliferyl-beta-D-galactopyranoside + H2O
4-methylumbelliferone + D-galactose
-
-
-
-
?
4-methylumbelliferyl-beta-D-glucopyranoside + H2O
4-methylumbelliferone + D-glucose
-
-
-
-
?
C6-4-nitrobenzo-2-oxa-1,3-diazole-galactosylceramide + H2O
C6-4-nitrobenzo-2-oxa-1,3-diazole-ceramide + D-galactose
-
-
-
-
?
C6-4-nitrobenzo-2-oxa-1,3-diazole-glucosylceramide + H2O
C6-4-nitrobenzo-2-oxa-1,3-diazole-ceramide + D-glucose
-
C6-NBD-glucosylceramide
-
-
?
glucosylceramide + H2O
ceramide + D-glucose
-
no activity with alpha-galactosylceramide, lactosylceramide, ganglioside M1a and sulfatides
-
-
?
p-nitrophenyl-beta-cellobioside + H2O
p-nitrophenyl-beta-D-glucoside + D-glucose
-
-
-
-
?
p-nitrophenyl-beta-lactoside + H2O
p-nitrophenyl-beta-D-glucoside + D-galactose
-
-
-
-
?
p-nitrophenyl-beta-maltoside + H2O
p-nitrophenol-beta-D-glucoside + D-glucose
-
-
-
-
?
2-nitrophenyl beta-D-galactopyranoside + H2O
2-nitrophenol + beta-D-galactose
-
-
-
?
2-nitrophenyl beta-D-galactopyranoside + H2O
2-nitrophenol + beta-D-galactose
-
-
-
?
4-nitrophenyl beta-D-galactopyranoside + H2O
4-nitrophenol + beta-D-galactose
-
-
-
?
4-nitrophenyl beta-D-galactopyranoside + H2O
4-nitrophenol + beta-D-galactose
-
low activity
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + beta-D-glucose
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + beta-D-glucose
-
-
-
?
4-O-beta-D-galactopyranosyl-D-glucopyranoside + H2O
D-galactose + beta-D-glucose
-
-
-
?
4-O-beta-D-galactopyranosyl-D-glucopyranoside + H2O
D-galactose + beta-D-glucose
-
-
-
?
4-O-beta-D-galactopyranosyl-D-glucopyranoside + H2O
D-galactose + beta-D-glucose
-
-
-
?
4-O-beta-D-galactopyranosyl-D-glucopyranoside + H2O
D-galactose + beta-D-glucose
-
-
-
?
4-O-beta-D-galactopyranosyl-D-glucopyranoside + H2O
D-galactose + beta-D-glucose
-
-
-
?
4-O-beta-D-galactopyranosyl-D-glucopyranoside + H2O
D-galactose + beta-D-glucose
-
-
-
?
4-O-beta-D-galactopyranosyl-D-glucopyranoside + H2O
D-galactose + beta-D-glucose
-
best substrate
-
?
4-O-beta-D-galactopyranosyl-D-glucopyranoside + H2O
D-galactose + beta-D-glucose
-
4fold higher activity for the N- and O-glycosylated than for the N-glycosylated molecule
-
?
4-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
cellobiose
-
?
4-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
cellobiose
-
?
6-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
gentiobiose
-
?
6-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
gentiobiose
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
4-O-beta-D-galactopyranosyl-D-glucopyranoside + H2O
D-galactose + beta-D-glucose
-
-
-
?
4-O-beta-D-galactopyranosyl-D-glucopyranoside + H2O
D-galactose + beta-D-glucose
-
-
-
?
4-O-beta-D-galactopyranosyl-D-glucopyranoside + H2O
D-galactose + beta-D-glucose
-
-
-
?
4-O-beta-D-galactopyranosyl-D-glucopyranoside + H2O
D-galactose + beta-D-glucose
-
-
-
?
4-O-beta-D-galactopyranosyl-D-glucopyranoside + H2O
D-galactose + beta-D-glucose
-
-
-
?
4-O-beta-D-galactopyranosyl-D-glucopyranoside + H2O
D-galactose + beta-D-glucose
-
-
-
?
4-O-beta-D-galactopyranosyl-D-glucopyranoside + H2O
D-galactose + beta-D-glucose
-
best substrate
-
?
4-O-beta-D-galactopyranosyl-D-glucopyranoside + H2O
D-galactose + beta-D-glucose
-
4fold higher activity for the N- and O-glycosylated than for the N-glycosylated molecule
-
?
4-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
cellobiose
-
?
4-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
cellobiose
-
?
6-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
gentiobiose
-
?
6-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
gentiobiose
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Tris(hydroxymethyl)aminomethane
-
competitive inhibition of lactase acitiviy, phlorizin activity not affected, Ki: 12 mM
additional information
-
coexpression with Rab4S22N or Rab11S25N decreases the number of vesicular structures positive for LPH. Trafficking delay of LPH following Rab protein depletion in MDCK cells
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
presence of Rab8T22NCFP results in an increase in LPHYFP-containing vesicular structures
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
4.64
(6-[N-(7-nitrobenz-2-oxa-1,3 diazol-4-yl)amino]hexanoyl)-beta-D-glucosylceramide
-
-
14
4-O-beta-D-galactopyranosyl-D-glucopyranoside
-
both mannose-rich precursor form and mature form
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.001875
-
activity in CHOP cell lysates transformed with cDNA encoding KlrP, with conduritol B epoxide, C6-4-nitrobenzo-2-oxa-1,3-diazole-glucosylceramide as substrate
0.00219
-
in cells infected with rhesus monkey rotavirus, in brush border-membrane enriched fraction
0.0028
-
in cells infected with rhesus monkey rotavirus and NSP4 neutralizing antibodies, in brush border-membrane enriched fraction
0.00359
-
in cells infected with inactivated rhesus monkey rotavirus, in brush border-membrane enriched fraction
0.00375
-
activity in CHOP cell lysates transformed with cDNA encoding KlrP, without conduritol B epoxide, C6-4-nitrobenzo-2-oxa-1,3-diazole-glucosylceramide as substrate
0.0052
-
activity in CHOP cell lysates transformed with cDNA encoding KlrP, with conduritol B epoxide, C6-4-nitrobenzo-2-oxa-1,3-diazole-galactosylceramide as substrate
0.0066
-
activity in CHOP cell lysates transformed with cDNA encoding KlrP, without conduritol B epoxide, C6-4-nitrobenzo-2-oxa-1,3-diazole-galactosylceramide as substrate
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
-
sequential passage of LPH through Rab4-, Rab8- and Rab11-containing compartments. Trafficking of LPH from the TGN to the cell surface can be modulated by dominant-negative Rab8
-
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
-
The profragment, LPHalpha, comprises homologous domains I and II and functions as an intramolecular chaperone in the context of the brush-border LPHbeta region of LPH
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). LPH_HUMAN
1927
1
218587
Swiss-Prot
Secretory Pathway (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
160000
215000
220000
220000
-
single-chain precursor, subsequently proteolytically processed to its active form, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
monomer
-
1 * 160000, SDS-PAGE, mature brush-border form after proteolytic cleavage of the precursor form
additional information
additional information
-
region LAC236 between R1647 and T1882 is implicated in the dimerization processof pro-enzyme
additional information
-
LPH encompasses four homologous domains, which presumably have evolved from two subsequent duplications of one ancestral gene, domain organization, overview. The profragment, LPHalpha, comprises homologous domains I and II and functions as an intramolecular chaperone in the context of the brush-border LPHbeta region of LPH. Inter-relationship between homologous domains III and IV of LPHbeta implication in the overall structure, function, and trafficking of LPH, overview. Isolated homologous domain III is transport-competent per se and sorted to the apical membrane in polarized cells. Nevertheless, it neither dimerizes nor acquires complete phlorizin hydrolase activity
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
proteolytic modification
-
pro-enzyme is cleaved in trans-Golgi network between Arg734 and Leu735, pro-region of enzyme is an intramolecular chaperone, analysis of processing and folding
glycoprotein
-
various modified glycoforms do not affect the transport from the Golgi to the cell surface
glycoprotein
-
processing of enzyme to a complex glycosylated protein increases in presence of pro-region
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D1711N
G1363S
-
the mutant protein is malfolded and enzymatically inactive and can not exit the endoplasmic reticulum. The mutation creates an additional N-glycosylation site that is characteristic of a temperature-sensitive protein. The potential glycosylation site generated by the mutation is not the cause of defective trafficking of LPH-G1363S or its reduced enzymatic activity. Intracellular transport and enzymatic activity, but not correct folding are partially restored by expression at 20°C. The mutant is responsible for an increased turnover rate
G1363S/N1361A
-
eliminates the N-glycosylation site, does not restore the features of wild-type LPH
I1697N
P1743S
additional information
D1711N
-
introduction of a glycosylation site, reduced transport rate to the plasma membrane
D1711N
-
introduction of potential N-glycosylation site, no enzymic activity, probably due to altered protein folding pattern and reduced dimerization efficiency
I1697N
-
introduction of a glycosylation site, reduced transport rate to the plasma membrane
I1697N
-
introduction of potential N-glycosylation site, no enzymic activity, probably due to altered protein folding pattern and reduced dimerization efficiency
P1743S
-
introduction of a glycosylation site, reduced transport rate to the plasma membrane
P1743S
-
introduction of potential N-glycosylation site, no enzymic activity, probably due to altered protein folding pattern and reduced dimerization efficiency
additional information
removal of domain I (LPHDELTA1) results in a malfolded ER-localized protein. Enzyme without domain II (LPHDELTA2) is normally transported along the secretory pathway, but does not dimerize nor is enzymatically active. The lactase activity is not detectable in LPHDELTA1 and LPHDELTA2. Phlorizin hydrolase activity is only detectable in LPHDELTA2, albeit at substantially reduced levels of 4.3%
additional information
-
loop-out mutagenesis and construction of deletion or individual domain forms of LPH. Removal of domain IV, which contains lactase, results in a diminished phlorizin hydrolase activity, lack of dimerization in the endoplasmic reticulum, but accelerated transport kinetics from the endoplasmic reticulum to the Golgi apparatus. By contrast, deletion of domain III, which harbors phlorizin hydrolase, generates a malfolded protein that is blocked in the endoplasmic reticulum. Transport kinetics and enzyme activity of LPH and deletion mutants differ
additional information
-
the naturally occurring polymorphism T13910C, i.e. rs4988235, causes lactose intolerance in the C-variant, associated with lower dietary calcium intake and serum calcium levels but not with BMD or fractures. Genotyping and phenotype, overview. The polymorphism is not associated with the genetic variations in the VDR gene, and no interactions between the two genotypes
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
of the recombinant protein by a hi-trap chelating HP column and superdex 200 column chromatography
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
COS-1 cells triple transfected with LPHCFP, SIYFP and Rab4, Rab8 or Rab11 fused to DsRed. MDCK cells stably expressing LPHmyc
-
expression in Chinese hamster ovary-derived cells expressing polyoma LT antigen, in HEK293 cells cotransfected with in KlrP siRNA, overexpression in Escherichia coli
-
mutant G1363S introduced into the wild-type LPH cDNA cloned in the vector pSG5. Mutant transiently expressed in COS-1 cells
-
transient expression of wild-type and domain deletion mutant enzymes and isolated enzyme domains in Cos-1 cells, expression in MDCK cells
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
medicine
-
rotavirus infection impairs LPH activity in intestinal cells, the decrease in enzyme activity is not Ca2+- and cAMP-dependent, the LPH biosynthesis, stability, and expression is not modified, the impairment of lactase enzymatic activity during rotavirus infection results from an inhibitory action of the secreted non-structural rotavirus protein NSP4
medicine
-
mutant form G1363S of LPH is involved in the pathogenesis of congenital lactase deficiency
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Jacob, R.; Weiner, J.R.; Stadge, S.; Naim, H.Y.
Additional N-glycosylation and its impact on the folding of intestinal lactase-phlorizin hydrolase
J. Biol. Chem.
275
10630-10637
2000
Homo sapiens
Wuthrich, M.; Sterchi, E.E.
Human lactase-phloizin hydrolase expressed in Cos-1 cells is proteolytically processed by the lysosomal pathway
FEBS Lett.
405
321-327
1997
Homo sapiens
Naim, H.Y.
The pro-region of human intestinale lactase-phlorizin hydrolase is enzymatically inactive towards lactose
Biol. Chem. Hoppe-Seyler
376
255-258
1995
Homo sapiens
Naim, H.Y.
Processing and transport of human small intestinal lactase-phlorizin hydrolase (LPH). Role of N-linked oligosaccharide modification
FEBS Lett.
342
302-307
1994
Homo sapiens
Naim, H.Y.; Lentze, M.J.
Impact of O-glycosylation on the function of human intestinal lactase-phlorizin hydrolase. Characterization of glycoforms varying in enzyme activity and localization of O-glycoside addition
J. Biol. Chem.
267
25494-25504
1992
Homo sapiens
Mantei, N.; Villa, M.; Enzler, T.; Wacker, H.; Boll, W.; James, P.; Hunziker, W.; Semenza, G.
Complete primary structure of human and rabbit lactase-phlorizin hydrolase: implications for biosynthesis, membrane anchoring and evolution of the enzyme
EMBO J.
7
2705-2713
1988
Homo sapiens, Oryctolagus cuniculus
Naim, H.Y.; Sterchi, E.E.; Lentze, M.J.
Biosynthesis and maturation of lactase-phlorizin hydrolase in the human small intestinal epithelial
Biochem. J.
241
427-434
1987
Homo sapiens
Skovbjerg, H.; Danielsen, E.M.; Noren, O.; Sjstrm, H.
Evidence for biosynthesis of lactase-phlorizin hydrolase as a single-chain high-molecular weight precursor
Biochim. Biophys. Acta
798
247-251
1984
Homo sapiens
Skovbjerg, H.; Sjstrm, H.; Noren, O.
Purification and characterization of amphiphilic lactase/phlorizin hydrolase from human small intestine
Eur. J. Biochem.
114
653-661
1981
Homo sapiens
Skovbjerg, H.; Noren, O.; Sjstrm, H.; Danielsen, E.M.; Enevoldsen, B.S.
Further characterization of intestinal lactase/phlorizin hydrolase
Biochim. Biophys. Acta
707
89-97
1982
Homo sapiens, Sus scrofa
Jacob, R.; Peters, K.; Naim, H.Y.
Prosequence of human lactase-phlorizin hydrolase modulates the folding of mature enzyme
J. Biol. Chem.
277
8217-8225
2002
Homo sapiens
Mizuma, T.; Fuseda, N.; Hayashi, M.
Kinetic characterization of glycosidase activity from disaccharide conjugate to monosaccharide conjugate in Caco-2 cells
J. Pharm. Pharmacol.
57
661-664
2005
Homo sapiens
Beau, I.; Cotte-Laffitte, J.; Geniteau-Legendre, M.; Estes, M.K.; Servin, A.L.
An NSP4-dependant mechanism by which rotavirus impairs lactase enzymatic activity in brush border of human enterocyte-like Caco-2 cells
Cell. Microbiol.
9
2254-2266
2007
Homo sapiens
Hayashi, Y.; Okino, N.; Kakuta, Y.; Shikanai, T.; Tani, M.; Narimatsu, H.; Ito, M.
Klotho-related protein is a novel cytosolic neutral beta-glycosylceramidase
J. Biol. Chem.
282
30889-30900
2007
Danio rerio, Homo sapiens, Mus musculus, Rattus norvegicus, Tetraodontidae
Behrendt, M.; Keiser, M.; Hoch, M.; Naim, H.Y.
Impaired trafficking and subcellular localization of a mutant lactase associated with congenital lactase deficiency
Gastroenterology
136
2295-2303
2009
Homo sapiens
Cramm-Behrens, C.I.; Dienst, M.; Jacob, R.
Apical cargo traverses endosomal compartments on the passage to the cell surface
Traffic
9
2206-2220
2008
Homo sapiens
Behrendt, M.; Polaina, J.; Naim, H.Y.
Structural hierarchy of regulatory elements in the folding and transport of an intestinal multidomain protein
J. Biol. Chem.
285
4143-4152
2010
Homo sapiens
Koek, W.; van Meurs, J.; van der Eerden, B.; Rivadeneira, F.; Zillikens, M.; Hofman, A.; Obermayer-Pietsch, B.; Lips, P.; Pols, H.; Uitterlinden, A.; van Leeuwen, J.
The T-13910C polymorphism in the lactase phlorizin hydrolase gene is associated with differences in serum calcium levels and calcium intake
J. Bone Miner. Res.
25
1980-1987
2010
Homo sapiens
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