Information on EC 3.1.1.63 - 11-cis-retinyl-palmitate hydrolase:
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The expected taxonomic range for this enzyme is: Amniota

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EC NUMBERCOMMENTARY
3.1.1.63-

RECOMMENDED NAMEGeneOntology No.
11-cis-retinyl-palmitate hydrolaseGO:0047520

REACTIONREACTION DIAGRAMCOMMENTARYORGANISM UNIPROT ACCESSION NO.LITERATURE
11-cis-retinyl palmitate + H2O = 11-cis-retinol + palmitate
show the reaction diagram		----

REACTION TYPEORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
hydrolysis of carboxylic ester----

PATHWAYKEGG LinkMetaCyc Link
Retinol metabolism00830 -

SYSTEMATIC NAMEIUBMB Comments
11-cis-retinyl-palmitate acylhydrolaseActivated by bile salts.

SYNONYMSORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
No entries in this field

CAS REGISTRY NUMBERCOMMENTARY
106389-23-5-

ORGANISMCOMMENTARYLITERATURESEQUENCE CODESEQUENCE DB SOURCE
Bos taurus-170640, 170657, 170660, 170681--Manually annotated by BRENDA team
Gallus gallus-170654--Manually annotated by BRENDA team
Homo sapiens-170637--Manually annotated by BRENDA team

GENERAL INFORMATIONORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
No entries in this field

SUBSTRATEPRODUCT                      REACTION DIAGRAMORGANISM UNIPROT ACCESSION NO. COMMENTARY/
Substrate		 LITERATURE/
Substrate		 COMMENTARY/
Product		 LITERATURE/
Product		 Reversibility
r=reversible
ir=irreversible
?=not specified
11-cis-retinyl palmitate + H2O11-cis-retinol + palmitate
show the reaction diagram		Homo sapiens--170637-170637?
11-cis-retinyl palmitate + H2O11-cis-retinol + palmitate
show the reaction diagram		Bos taurus--170640-170640?
11-cis-retinyl palmitate + H2O11-cis-retinol + palmitate
show the reaction diagram		Bos taurus--170657-170657?
11-cis-retinyl palmitate + H2O11-cis-retinol + palmitate
show the reaction diagram		Bos taurus--170660-170660?
11-cis-retinyl palmitate + H2O11-cis-retinol + palmitate
show the reaction diagram		Bos taurus--170681-170681?
11-cis-retinyl palmitate + H2O11-cis-retinol + palmitate
show the reaction diagram		Gallus gallus-all-trans-retinyl palmitate is hydrolyzed with higher specificity170654-170654?
additional information?-Bos taurus-the 11-cis-isomer is hydrolyzed at a much higher rate than the other isomers, 9-cis, 13-cis, and all-trans-retinyl palmitate, all-trans-retinyl palmitate and cholesteryl oleate may be hydrolyzed at the same non-specific catalytic site, it is very likely that 11-cis-retinyl palmitate is hydrolyzed at a discrete catalytic site170657---
additional information?-Bos taurus-also hydrolyzes all-trans-retinol with lower activity170640---
additional information?-Bos taurus-the hydrolysis of 11-cis retinyl esters in the retinal pigment epithelium membrane constitutes a novel pathway of visual chromophore biosynthesis170681---

NATURAL SUBSTRATESNATURAL PRODUCTSREACTION DIAGRAMORGANISM UNIPROT ACCESSION NO.COMMENTARY SUBSTRATELITERATURE
(Substrate)		COMMENTARY PRODUCTLITERATURE
(Product)
additional information?-Bos taurus-the hydrolysis of 11-cis retinyl esters in the retinal pigment epithelium membrane constitutes a novel pathway of visual chromophore biosynthesis170681--

COFACTORORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATUREIMAGE
No entries in this field

METALS and IONS ORGANISM UNIPROT ACCESSION NO.COMMENTARY LITERATURE
No entries in this field

INHIBITORSORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
all-trans-retinyl bromoacetateBos taurus-0.05 mM 50% inhibition170640 2D-image
NEMBos taurus-inhibits all-trans retinyl-palmitate hydrolase and 11-cis-retinyl-palmitate hydrolase activity of the liver enzyme, inhibits all-trans-retinyl-palmitate hydrolase activity of the pigment epithelium, 1-cis-retinyl-palmitate hydrolase activity of the pigment epithelium is unaffected170660 2D-image
trioleinBos taurus-inhibits all-trans retinyl-palmitate hydrolase and 11-cis-retinyl-palmitate hydrolase activity of the liver enzyme, inhibits all-trans-retinyl-palmitate hydrolase activity of the pigment epithelium, 1-cis-retinyl-palmitate hydrolase activity of the pigment epithelium is unaffected170660 2D-image
all-trans-retinyl palmitateHomo sapiens-weak inhibition170637 2D-image
additional informationBos taurus-the distinctive apparent inhibition constants for NEM-induced inhibition of 11-cis retinyl-palmitate hydrolase and the all-trans-retinyl-palmitate hydrolase activity suggest a fundamental difference in the amino acid composition at the active site of the enzyme(s)170660-

ACTIVATING COMPOUNDORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
additional informationHomo sapiens-no detergents required170637-

KM VALUE [mM]KM VALUE [mM] MaximumSUBSTRATEORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
0.004-11-cis-retinyl palmitateGallus gallus-enzyme from retinal pigment epithelium170654 2D-image
0.0185-11-cis-retinyl palmitateGallus gallus-enzyme from retina170654 2D-image
0.019-11-cis-retinyl palmitateHomo sapiens--170637 2D-image
0.66-11-cis-retinyl palmitateBos taurus--170640 2D-image

TURNOVER NUMBER [1/s] TURNOVER NUMBER MAXIMUM[1/s] SUBSTRATEORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
No entries in this field

kcat/KM VALUE [1/mMs-1]kcat/KM VALUE [1/mMs-1] MaximumSUBSTRATEORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
No entries in this field

Ki VALUE [mM]Ki VALUE [mM] MaximumINHIBITORORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
0.05-all-trans-retinyl bromoacetateBos taurus--170640 2D-image

IC50 VALUE [mM]IC50 VALUE [mM] MaximumINHIBITORORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
No entries in this field

SPECIFIC ACTIVITY [µmol/min/mg] SPECIFIC ACTIVITY MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
No entries in this field

pH OPTIMUMpH MAXIMUMORGANISM UNIPROT ACCESSION NO. COMMENTARYLITERATURE
89Bos taurus--170640
8.5-Homo sapiens-addition of 1.0% sodium taurocholate170637

pH RANGEpH RANGE MAXIMUMORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
79.5Homo sapiens-pH 7.0: about 60% of maximal activity, pH 9.5: about 30% of maximal activity170637

TEMPERATURE OPTIMUMTEMPERATURE OPTIMUM MAXIMUMORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
No entries in this field

TEMPERATURE RANGE TEMPERATURE MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
No entries in this field

pI VALUEpI VALUE MAXIMUMORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
No entries in this field

SOURCE TISSUE ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE SOURCE
liverBos taurus--170660Manually annotated by BRENDA team
retinaGallus gallus--170654Manually annotated by BRENDA team
retinal pigment epitheliumHomo sapiens--170637Manually annotated by BRENDA team
retinal pigment epitheliumGallus gallus-membrane170654Manually annotated by BRENDA team
retinal pigment epitheliumBos taurus--170640, 170657, 170660, 170681Manually annotated by BRENDA team

LOCALIZATION ORGANISM UNIPROT ACCESSION NO. COMMENTARY GeneOntology No. LITERATURE SOURCE
microsomeBos taurus---170640Manually annotated by BRENDA team
plasma membraneBos taurus--5886170657, 170681Manually annotated by BRENDA team

PDBSCOPCATHORGANISM
No entries in this field

MOLECULAR WEIGHT MOLECULAR WEIGHT MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
No entries in this field

SUBUNITS ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
No entries in this field

POSTTRANSLATIONAL MODIFICATION ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
No entries in this field

Crystallization/COMMENTARY ORGANISM UNIPROT ACCESSION NO. LITERATURE
No entries in this field

pH STABILITYpH STABILITY MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
No entries in this field

TEMPERATURE STABILITYTEMPERATURE STABILITY MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARYLITERATURE
50-Homo sapiens-10 min, complete loss of activity170637

GENERAL STABILITYORGANISM UNIPROT ACCESSION NO.LITERATURE
No entries in this field

ORGANIC SOLVENT ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
No entries in this field

OXIDATION STABILITY ORGANISM UNIPROT ACCESSION NO. LITERATURE
No entries in this field

STORAGE STABILITY ORGANISM UNIPROT ACCESSION NO. LITERATURE
-20°C, overnight storage of cell homogenate, no loss of activityHomo sapiens-170637

Purification/COMMENTARY ORGANISM UNIPROT ACCESSION NO. LITERATURE
No entries in this field

Cloned/COMMENTARY ORGANISM UNIPROT ACCESSION NO. LITERATURE
No entries in this field

EXPRESSION ORGANISM UNIPROT ACCESSION NO. LITERATURE
No entries in this field

ENGINEERINGORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
No entries in this field

Renatured/COMMENTARYORGANISM UNIPROT ACCESSION NO.LITERATURE
No entries in this field

APPLICATIONORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
No entries in this field

DISEASETITLE OF PUBLICATIONLINK TO PUBMED
No entries in this field

REF. AUTHORS TITLE JOURNAL VOL. PAGES YEAR ORGANISM (UNIPROT ACCESSION NO.)LINK TO PUBMEDSOURCE
170637Blaner, W.S.; Das, S.R.; Gouras, P.; Flood, M.T.Hydrolysis of 11-cis- and all-trans-retinyl palmitate by homogenates of human retinal epithelial cellsJ. Biol. Chem.26253-581987Homo sapiens PubMed
170640Blaner W.S.; Prystowsky, J.H.; Smith, J.E.; Goodman, D.S.Rat liver retinyl palmitate hydrolase activity. Relationship to cholesteryl oleate and triolein hydrolase activitiesBiochim. Biophys. Acta794419-4271984Bos taurus PubMed
170654Bustamante, J.J.; Ziari, S.; Ramirez, R.D.; Tsin, A.T.C.Retinyl ester hydrolase and the visual cycle in the chicken eyeAm. J. Physiol.269R1346-R13501995Gallus gallus PubMed
170657Mata, J.R.; Mata, N.L.; Tsin, A.T.C.Substrate specificity of retinyl ester hydrolase activity in retinal pigment epitheliumJ. Lipid Res.39604-6121998Bos taurus PubMed
170660Mata, N.L.; Mata, J.R.; Tsin, A.T.C.Comparison of retinyl ester hydrolase activities in bovine liver and retinal pigment epitheliumJ. Lipid Res.371947-19521996Bos taurus PubMed
170681Mata, N.L.; Tsin, A.T.C.Distribution of 11-cis LRAT, 11-cis RD and 11-cis REH in bovine retinal pigment epithelium membranesBiochim. Biophys. Acta139416-221998Bos taurus PubMed

LINKS TO OTHER DATABASES (specific for EC-Number 3.1.1.63)
ExplorEnz
ExPASy
KEGG
MetaCyc
NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM
IUBMB Enzyme Nomenclature
PROSITE Database of protein families and domains
SYSTERS
Protein Mutant Database
InterPro (database of protein families, domains and functional sites)