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show all sequences of 1.8.3.5

Prenylcysteine lyase deficiency in mice results in the accumulation of farnesylcysteine and geranylgeranylcysteine in brain and liver

Beigneux, A.; Withycombe, S.K.; Digits, J.A.; Tschantz, W.R.; Weinbaum, C.A.; Griffey, S.M.; Bergo, M.; Casey, P.J.; Young, S.G.; J. Biol. Chem. 277, 38358-38363 (2002)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
-
Mus musculus
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
S-prenyl-L-cysteine + O2 + H2O
Mus musculus
physiologic role in cleaving prenylcysteines in mammals, cleaves the thioether bond of prenylcysteines to yield free cysteine and the aldehyde of the isoprenoid lipid
prenal + L-cysteine + H2O2
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Mus musculus
Q9CQF9
mouse, wild type and knockout mutants
-
Source Tissue
Source Tissue
Commentary
Organism
Textmining
brain
-
Mus musculus
-
heart
-
Mus musculus
-
kidney
-
Mus musculus
-
liver
-
Mus musculus
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
farnesyl-L-cysteine + O2 + H2O
-
437708
Mus musculus
farnesal + L-cysteine + H2O2
-
-
-
?
geranylgeranyl-L-cysteine + O2 + H2O
-
437708
Mus musculus
geranylgeranal + L-cysteine + H2O2
-
-
-
?
S-prenyl-L-cysteine + O2 + H2O
-
437708
Mus musculus
prenal + L-cysteine + H2O2
-
437708
Mus musculus
?
S-prenyl-L-cysteine + O2 + H2O
physiologic role in cleaving prenylcysteines in mammals, cleaves the thioether bond of prenylcysteines to yield free cysteine and the aldehyde of the isoprenoid lipid
437708
Mus musculus
prenal + L-cysteine + H2O2
-
-
-
?
Temperature Optimum [C]
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
37
-
assay at
Mus musculus
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.7
-
assay at
Mus musculus
Cloned(Commentary) (protein specific)
Commentary
Organism
-
Mus musculus
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
S-prenyl-L-cysteine + O2 + H2O
Mus musculus
physiologic role in cleaving prenylcysteines in mammals, cleaves the thioether bond of prenylcysteines to yield free cysteine and the aldehyde of the isoprenoid lipid
prenal + L-cysteine + H2O2
-
-
?
Source Tissue (protein specific)
Source Tissue
Commentary
Organism
Textmining
brain
-
Mus musculus
-
heart
-
Mus musculus
-
kidney
-
Mus musculus
-
liver
-
Mus musculus
-
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
farnesyl-L-cysteine + O2 + H2O
-
437708
Mus musculus
farnesal + L-cysteine + H2O2
-
-
-
?
geranylgeranyl-L-cysteine + O2 + H2O
-
437708
Mus musculus
geranylgeranal + L-cysteine + H2O2
-
-
-
?
S-prenyl-L-cysteine + O2 + H2O
-
437708
Mus musculus
prenal + L-cysteine + H2O2
-
437708
Mus musculus
?
S-prenyl-L-cysteine + O2 + H2O
physiologic role in cleaving prenylcysteines in mammals, cleaves the thioether bond of prenylcysteines to yield free cysteine and the aldehyde of the isoprenoid lipid
437708
Mus musculus
prenal + L-cysteine + H2O2
-
-
-
?
Temperature Optimum [C] (protein specific)
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
37
-
assay at
Mus musculus
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.7
-
assay at
Mus musculus
Other publictions for EC 1.8.3.5
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [C]
Temperature Range [C]
Temperature Stability [C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [C] (protein specific)
Temperature Range [C] (protein specific)
Temperature Stability [C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
743865
Dashty
Proteome of human plasma very ...
Homo sapiens
Thromb. Haemost.
111
518-530
2014
-
-
-
-
-
-
-
-
1
-
-
-
-
2
-
-
-
-
-
1
-
-
1
-
-
-
-
-
-
-
-
-
-
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-
-
-
-
-
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-
1
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-
-
-
-
-
-
-
1
-
-
1
-
-
-
-
-
-
-
-
-
-
1
1
-
-
-
710018
Huizinga
Farnesylcysteine lyase is invo ...
Arabidopsis thaliana
Mol. Plant
3
143-155
2010
-
-
1
-
1
-
6
1
2
-
3
1
-
2
-
1
-
1
-
-
-
-
2
1
1
-
-
-
1
-
-
1
-
-
5
-
-
1
1
-
1
-
5
6
-
1
2
-
3
1
-
-
1
-
-
-
-
-
2
1
1
-
-
-
1
-
-
-
-
2
2
-
-
-
706670
Banfi
Proteomic analysis of human lo ...
Homo sapiens
Proteomics
9
1344-1352
2009
-
-
-
-
-
-
1
-
-
-
1
-
-
2
-
-
-
-
-
1
-
-
1
-
1
-
-
-
-
-
-
1
-
-
-
-
-
-
1
-
-
-
-
1
-
-
-
-
1
-
-
-
-
-
-
1
-
-
1
-
1
-
-
-
-
-
-
-
-
1
1
-
-
-
710279
Crowell
Arabidopsis thaliana plants po ...
Arabidopsis thaliana, Arabidopsis thaliana Col-0
Plant J.
50
839-847
2007
-
-
1
-
1
-
-
-
1
-
-
2
-
5
-
-
-
-
-
1
-
-
4
-
1
-
-
-
1
-
-
-
-
-
-
-
-
1
-
-
1
-
-
-
-
-
1
-
-
2
-
-
-
-
-
1
-
-
4
-
1
-
-
-
1
-
-
-
-
3
3
-
-
-
667445
Wouters
Downregulation of two novel ge ...
Mus musculus
Biochem. Biophys. Res. Commun.
346
491-500
2006
-
-
-
-
-
-
-
-
-
-
-
-
-
3
-
-
-
-
-
1
-
-
3
-
-
-
-
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-
-
-
-
-
-
-
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-
-
-
-
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-
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-
1
-
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3
-
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-
-
-
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-
669763
Lu
Thematic review series: lipid ...
Bos taurus
J. Lipid Res.
47
1352-1357
2006
1
-
-
-
-
-
-
2
1
-
1
-
-
1
-
-
1
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1
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3
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-
-
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1
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2
1
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1
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-
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-
1
-
1
-
-
3
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
437708
Beigneux
Prenylcysteine lyase deficienc ...
Mus musculus
J. Biol. Chem.
277
38358-38363
2002
-
-
1
-
-
-
-
-
-
-
-
1
-
4
-
-
-
-
-
6
-
-
4
-
1
-
-
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
6
-
-
4
-
1
-
-
-
1
-
-
-
-
-
-
-
-
-
437709
Digits
Stereospecificity and kinetic ...
Homo sapiens
J. Biol. Chem.
277
41086-41093
2002
-
-
-
-
-
-
2
2
-
-
-
1
-
2
-
-
-
-
-
-
-
-
3
-
1
-
-
1
1
-
-
1
-
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1
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2
-
2
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1
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3
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1
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1
1
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