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Information on EC 3.7.1.4 - phloretin hydrolase and Organism(s) Homo sapiens and UniProt Accession P09848

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     3 Hydrolases
         3.7 Acting on carbon-carbon bonds
             3.7.1 In ketonic substances
                3.7.1.4 phloretin hydrolase
IUBMB Comments
Also hydrolyses other C-acylated phenols related to phloretin. Isolated from the fungus Aspergillus niger and the bacteria Pantoea agglomerans and Eubacterium ramulus.
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This record set is specific for:
Homo sapiens
UNIPROT: P09848
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Word Map
The taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
phloretin hydrolase, png hydrolase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
lactase-phlorizin hydrolase
-
phloretin hydrolase
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C-acylphenol acylhydrolase
-
-
-
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lactase phlorizin-hydrolase
-
-
lactase-phlorizin hydrolase
phloretin hydrolase
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-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
phloretin + H2O = phloretate + phloroglucinol
show the reaction diagram
also hydrolyses other C-acetylated phenols related to phloretin
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of C-C bond
-
ester hydrolysis
-
-
hydrolysis of C-C bond
SYSTEMATIC NAME
IUBMB Comments
phloretin acylhydrolase (phloroglucinol forming)
Also hydrolyses other C-acylated phenols related to phloretin. Isolated from the fungus Aspergillus niger and the bacteria Pantoea agglomerans and Eubacterium ramulus.
CAS REGISTRY NUMBER
COMMENTARY hide
37289-38-6
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
lactose + H2O
D-glucose + D-galactose
show the reaction diagram
-
-
-
?
phloretin + H2O
phloretate + phloroglucinol
show the reaction diagram
-
-
-
?
lactose + H2O
beta-D-galactose + beta-D-glucose
show the reaction diagram
-
-
-
-
?
lactose + H2O
D-galactose + D-glucose
show the reaction diagram
-
-
-
-
?
lactose + H2O
D-glucose + D-galactose
show the reaction diagram
-
-
-
-
?
lactose + H2O
glucose + galactose
show the reaction diagram
-
-
-
-
?
phloretin + H2O
phloretate + phloroglucinol
show the reaction diagram
-
-
-
-
?
phlorhizin + H2O
3-(4-hydroxyphenyl)propanoate + arbutin
show the reaction diagram
-
-
-
-
?
additional information
?
-
-
the enzyme interacts with ER chaperones, immunglobulin binding protein, and calnexin at non-permissive temperatures in the ER
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
phloretin + H2O
phloretate + phloroglucinol
show the reaction diagram
-
-
-
?
phloretin + H2O
phloretate + phloroglucinol
show the reaction diagram
-
-
-
-
?
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
intestinal villus
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
the recombinant precusor in COS-1 cells resides in the ER, not mature wild-type
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
LPH_HUMAN
1927
1
218587
Swiss-Prot
other Location (Reliability: 5)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
250000
-
gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
-
-
additional information
-
the mature enzyme shows a temperature-sensitive conformation, interaction with ER chaperones, immunglobulin binding protein, and calnexin, enzyme structure, overview
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
proteolytic modification
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enzyme is sythesized as a transport-competent precursor, i.e. pro-LPH, intracellular cleavage process in the trans-Golgi network between Arg734 and Leu 735 to yield the mature enzyme, i.e. LPHbetainitial, the propeptide of the zymogen, i.e. LPHalpha, modulates as a chaperone the folding of the mature enzyme after it has been cleaved off, mechanism, overview
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
N1340Q
-
the variant lacks the closest potential N-glycosylation site to Asp1338
N1814Q
-
the variant lacks the N-glycosylation site in the domain IV
N821Q
-
the variant lacks the N-glycosylation site in the domain II
additional information
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
the mature enzyme shows a temperature-sensitive conformation
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant mature enzyme and pro-enzyme from COS-1 cells
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in COS-1 cells
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the C/T-13910 SNP in the gene encoding lactase-phlorizin hydrolase on chromosome 2 defines adult-type hypolactasia status. Study in young finns analysing association of adult-type hypolactasia with coronary artery disease risk factors and with with markers of early atherosclerosis respectively
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transient expression of mature enzyme and pro-enzyme in COS-1 cells, in vitro transcritption and translation
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
adult-type hypolactasia is characterized by a fall of lactase activity levels to 5 - 10% of birth levels occuring during childhood and adolescence
medicine
molecular biology
-
LPH and PNGH enzymes have the same genomic origin, but differ in transcriptional and, possibly, post-translational processing
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Manually annotated by BRENDA team
Tseung, C.W.; McMahon, L.G.; Vazquez, J.; Pohl, J.; Gregory, J.F.
Partial amino acid sequence and mRNA analysis of cytosolic pyridoxine-beta-D-glucoside hydrolase from porcine intestinal mucosa: proposed derivation from the lactase-phlorizin hydrolase gene
Biochem. J.
380
211-218
2004
Homo sapiens, Oryctolagus cuniculus
Manually annotated by BRENDA team
Bodlaj, G.; Stoecher, M.; Hufnagl, P.; Hubmann, R.; Biesenbach, G.; Stekel, H.; Berg, J.
Genotyping of the lactase-phlorizin hydrolase -13910 polymorphism by lightCycler PCR and implications for the diagnosis of lactose intolerance
Clin. Chem.
52
148-151
2006
Homo sapiens
Manually annotated by BRENDA team
Bulhoes, A.C.; Goldani, H.A.; Oliveira, F.S.; Matte, U.S.; Mazzuca, R.B.; Silveira, T.R.
Correlation between lactose absorption and the C/T-13910 and G/A-22018 mutations of the lactase-phlorizin hydrolase (LCT) gene in adult-type hypolactasia
Braz. J. Med. Biol. Res.
40
1441-1446
2007
Homo sapiens (P09848)
Manually annotated by BRENDA team
Piepoli, A.; Schirru, E.; Mastrorilli, A.; Gentile, A.; Cotugno, R.; Quitadamo, M.; Merla, A.; Congia, M.; Usai Satta, P.; Perri, F.
Genotyping of the lactase-phlorizin hydrolase c/t-13910 polymorphism by means of a new rapid denaturing high-performance liquid chromatography-based assay in healthy subjects and colorectal cancer patients
J. Biomol. Screen.
12
733-739
2007
Homo sapiens
Manually annotated by BRENDA team
Lehtimaeki, T.; Hutri-Kaehoenen, N.; Kaehoenen, M.; Hemminki, J.; Mikkilae, V.; Laaksonen, M.; Raesaenen, L.; Mononen, N.; Juonala, M.; Marniemi, J.; Viikari, J.; Raitakari, O.
Adult-type hypolactasia is not a predisposing factor for the early functional and structural changes of atherosclerosis: the Cardiovascular Risk in Young Finns Study
Clin. Sci.
115
265-271
2008
Homo sapiens
Manually annotated by BRENDA team
Diekmann, L.; Behrendt, M.; Amiri, M.; Naim, H.Y.
Structural determinants for transport of lactase phlorizin-hydrolase in the early secretory pathway as a multi-domain membrane glycoprotein
Biochim. Biophys. Acta
1861
3119-3128
2017
Homo sapiens
Manually annotated by BRENDA team