Enzymes
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Name help_outline
an S-prenyl-L-cysteine
Identifier
CHEBI:137935
Charge
0
Formula
(C5H8)n.C8H15NO2S
Search links
Involved in 3 reaction(s)
Find proteins in UniProtKB for this molecule
Form(s) in this reaction:
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Identifier: RHEA-COMP:13676Polymer name: an S-prenyl-L-cysteinePolymerization index help_outline nFormula C8H15NO2S(C5H8)nCharge (0)(0)nMol File for the polymer
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- Name help_outline H2O Identifier CHEBI:15377 (Beilstein: 3587155; CAS: 7732-18-5) help_outline Charge 0 Formula H2O InChIKeyhelp_outline XLYOFNOQVPJJNP-UHFFFAOYSA-N SMILEShelp_outline [H]O[H] 2D coordinates Mol file for the small molecule Search links Involved in 6,048 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline O2 Identifier CHEBI:15379 (CAS: 7782-44-7) help_outline Charge 0 Formula O2 InChIKeyhelp_outline MYMOFIZGZYHOMD-UHFFFAOYSA-N SMILEShelp_outline O=O 2D coordinates Mol file for the small molecule Search links Involved in 2,648 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
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Name help_outline
polyprenal
Identifier
CHEBI:137934
Charge
0
Formula
(C5H8)n.C5H8O
Search links
Involved in 10 reaction(s)
Find proteins in UniProtKB for this molecule
Form(s) in this reaction:
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Identifier: RHEA-COMP:13675Polymer name: a prenalPolymerization index help_outline nFormula C5H8O(C5H8)nCharge (0)(0)nMol File for the polymer
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- Name help_outline H2O2 Identifier CHEBI:16240 (Beilstein: 3587191; CAS: 7722-84-1) help_outline Charge 0 Formula H2O2 InChIKeyhelp_outline MHAJPDPJQMAIIY-UHFFFAOYSA-N SMILEShelp_outline [H]OO[H] 2D coordinates Mol file for the small molecule Search links Involved in 426 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline L-cysteine Identifier CHEBI:35235 Charge 0 Formula C3H7NO2S InChIKeyhelp_outline XUJNEKJLAYXESH-REOHCLBHSA-N SMILEShelp_outline [NH3+][C@@H](CS)C([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 59 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
RHEA:53892 | RHEA:53893 | RHEA:53894 | RHEA:53895 | |
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Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
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Specific form(s) of this reaction
Publications
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Isolation and characterization of a prenylcysteine lyase from bovine brain.
Zhang L., Tschantz W.R., Casey P.J.
Prenylated proteins contain one of two isoprenoid lipids, either the 15-carbon farnesyl or the 20-carbon geranylgeranyl, covalently attached to cysteine residues at or near their C terminus. The cellular abundance of prenylated proteins, which can comprise up to 2% of total cellular protein, raise ... >> More
Prenylated proteins contain one of two isoprenoid lipids, either the 15-carbon farnesyl or the 20-carbon geranylgeranyl, covalently attached to cysteine residues at or near their C terminus. The cellular abundance of prenylated proteins, which can comprise up to 2% of total cellular protein, raises the question of how cells dispose of prenylcysteines produced during the normal turnover of prenylated proteins. We have identified and characterized a novel enzyme, which we term prenylcysteine lyase, that is capable of cleaving the thioether bond of prenylcysteines. The enzyme was isolated from bovine brain membranes and exhibits an apparent molecular mass of 63 kDa. The enzyme did not require NADPH as cofactor for prenylcysteine degradation, thus distinguishing it from cytochrome P450- and flavin-containing monooxygenases that catalyze S-oxidation of thioethers. Purified prenylcysteine lyase shows similar kinetics in utilization of both farnesylcysteine and geranylgeranylcysteine as substrates, although Vmax is 2-fold higher with the former compound. Interaction of prenylcysteine substrates with the enzyme requires that they possess a free amino group; N-acetylated prenylcysteines and prenyl peptides are not substrates. These findings suggest that prenylcysteine lyase is a specific enzyme involved in prenylcysteine metabolism in mammalian cells, most likely comprising the final step in the degradation of prenylated proteins. << Less
J. Biol. Chem. 272:23354-23359(1997) [PubMed] [EuropePMC]
This publication is cited by 1 other entry.
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Lysosomal prenylcysteine lyase is a FAD-dependent thioether oxidase.
Tschantz W.R., Digits J.A., Pyun H.J., Coates R.M., Casey P.J.
Prenylated proteins contain either a 15-carbon farnesyl or a 20-carbon geranylgeranyl isoprenoid covalently attached via a thioether bond to a cysteine residue at or near their C terminus. As prenylated proteins comprise up to 2% of the total protein in eukaryotic cells, and the thioether bond is ... >> More
Prenylated proteins contain either a 15-carbon farnesyl or a 20-carbon geranylgeranyl isoprenoid covalently attached via a thioether bond to a cysteine residue at or near their C terminus. As prenylated proteins comprise up to 2% of the total protein in eukaryotic cells, and the thioether bond is a stable modification, their degradation raises a metabolic challenge to cells. A lysosomal enzyme termed prenylcysteine lyase has been identified that cleaves prenylcysteines to cysteine and an unidentified isoprenoid product. Here we show that the isoprenoid product of prenylcysteine lyase is the C-1 aldehyde of the isoprenoid moiety (farnesal in the case of C-15). The enzyme requires molecular oxygen as a cosubstrate and utilizes a noncovalently bound flavin cofactor in an NAD(P)H-independent manner. Additionally, a stoichiometric amount of hydrogen peroxide is produced during the reaction. These surprising findings indicate that prenylcysteine lyase utilizes a novel oxidative mechanism to cleave thioether bonds and provide insight into the unique role this enzyme plays in the cellular metabolism of prenylcysteines. << Less
J. Biol. Chem. 276:2321-2324(2001) [PubMed] [EuropePMC]
This publication is cited by 2 other entries.