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UniProtKB:Accession Number | P35127 | P15374 |
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Entry name | UBL1_YEAST | UCHL3_HUMAN |
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Activity | Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C- terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal). | Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C- terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal). |
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Subunit |
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Subcellular location |
| Cytoplasm. |
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Cofactor |
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Compound table: links to PDB-related databases & PoSSuM |
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| Substrates | Products | intermediates |
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KEGG-id | C04090 | C03635 | C00001 | C00496 | C00145 | C02188 | I00153 | I00154 | I00155 |
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E.C. | 3.1.2.15 | 3.4.19.12 | 3.1.2.15,3.4.19.12 | 3.1.2.15,3.4.19.12 | 3.1.2.15 | 3.4.19.12 | 3.4.19.12 | 3.4.19.12 | 3.4.19.12 |
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Compound | Ubiquitin C-terminal thiolester | Protein N-ubiquityllysine | H2O | Ubiquitin | Thiol | Protein lysine | Peptidyl-Cys-tetrahedral-intermediate (with previous peptide) | Acyl-enzyme(Peptidyl-Cys-acyl group) | Peptidyl-Cys-tetrahedral-intermediate |
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Type | carbohydrate,peptide/protein,sulfide group | amide group,lipid,peptide/protein | H2O | peptide/protein | sulfhydryl group | amine group,lipid,peptide/protein |
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ChEBI |
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| 15377
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PubChem |
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| 22247451 962
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1cmxA |  |  |  |  |  |  |  | Unbound | Unbound | | Unbound | Unbound | Unbound | Unbound | Intermediate-analogue:GLZ 376(chain B) | Unbound |
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1cmxC |  |  |  |  |  |  |  | Unbound | Unbound | | Unbound | Unbound | Unbound | Unbound | Intermediate-analogue:GLZ 776(chain D) | Unbound |
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1uchA |  |  |  |  |  |  |  | Unbound | Unbound | | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
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1xd3A |  |  |  |  |  |  |  | Unbound | Unbound | | Unbound | Unbound | Unbound | Transition-state-analogue:GVE | Unbound | Unbound |
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1xd3C |  |  |  |  |  |  |  | Unbound | Unbound | | Unbound | Unbound | Unbound | Transition-state-analogue:GVE | Unbound | Unbound |
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References for Catalytic Mechanism | References | Sections | No. of steps in catalysis |
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[2] | FIG 1, p.487-499 |
| [4] | p.3789-3791 |
| [8] | Fig.3, p.3878 |
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references | [1] |
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PubMed ID | 2532544 |
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Journal | Biochemistry |
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Year | 1989 |
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Volume | 28 |
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Pages | 8530-6 |
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Authors | Duerksen-Hughes PJ, Williamson MM, Wilkinson KD |
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Title | Affinity chromatography using protein immobilized via arginine residues: purification of ubiquitin carboxyl-terminal hydrolases. |
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[2] |
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PubMed ID | 7845227 |
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Journal | Methods Enzymol |
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Year | 1994 |
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Volume | 244 |
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Pages | 486-500 |
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Authors | Storer AC, Menard R |
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Title | Catalytic mechanism in papain family of cysteine peptidases. |
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[3] |
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PubMed ID | 8639624 |
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Journal | Biochemistry |
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Year | 1996 |
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Volume | 35 |
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Pages | 6735-44 |
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Authors | Larsen CN, Price JS, Wilkinson KD |
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Title | Substrate binding and catalysis by ubiquitin C-terminal hydrolases: identification of two active site residues. |
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[4] |
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Comments | X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS). |
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PubMed ID | 9233788 |
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Journal | EMBO J |
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Year | 1997 |
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Volume | 16 |
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Pages | 3787-96 |
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Authors | Johnston SC, Larsen CN, Cook WJ, Wilkinson KD, Hill CP |
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Title | Crystal structure of a deubiquitinating enzyme (human UCH-L3) at 1.8 A resolution. |
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Related PDB | 1uch |
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Related UniProtKB | P15374 |
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[5] |
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PubMed ID | 9485312 |
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Journal | Biochemistry |
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Year | 1998 |
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Volume | 37 |
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Pages | 1868-79 |
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Authors | Dang LC, Melandri FD, Stein RL |
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Title | Kinetic and mechanistic studies on the hydrolysis of ubiquitin C-terminal 7-amido-4-methylcoumarin by deubiquitinating enzymes. |
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[6] |
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PubMed ID | 10413498 |
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Journal | Biochemistry |
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Year | 1999 |
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Volume | 38 |
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Pages | 9242-53 |
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Authors | Rajesh S, Sakamoto T, Iwamoto-Sugai M, Shibata T, Kohno T, Ito Y |
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Title | Ubiquitin binding interface mapping on yeast ubiquitin hydrolase by NMR chemical shift perturbation. |
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[7] |
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PubMed ID | 10512618 |
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Journal | Biochemistry |
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Year | 1999 |
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Volume | 38 |
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Pages | 11634-42 |
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Authors | Sakamoto T, Tanaka T, Ito Y, Rajesh S, Iwamoto-Sugai M, Kodera Y, Tsuchida N, Shibata T, Kohno T |
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Title | An NMR analysis of ubiquitin recognition by yeast ubiquitin hydrolase: evidence for novel substrate recognition by a cysteine protease. |
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[8] |
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Comments | X-ray crystallography |
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PubMed ID | 10406793 |
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Journal | EMBO J |
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Year | 1999 |
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Volume | 18 |
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Pages | 3877-87 |
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Authors | Johnston SC, Riddle SM, Cohen RE, Hill CP |
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Title | Structural basis for the specificity of ubiquitin C-terminal hydrolases. |
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Related PDB | 1cmx |
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Related UniProtKB | P35127 |
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[9] |
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PubMed ID | 10518943 |
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Journal | J Mol Biol |
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Year | 1999 |
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Volume | 291 |
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Pages | 1067-77 |
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Authors | Wilkinson KD, Laleli-Sahin E, Urbauer J, Larsen CN, Shih GH, Haas AL, Walsh ST, Wand AJ |
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Title | The binding site for UCH-L3 on ubiquitin: mutagenesis and NMR studies on the complex between ubiquitin and UCH-L3. |
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[10] |
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PubMed ID | 10893261 |
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Journal | J Cell Biol |
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Year | 2000 |
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Volume | 150 |
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Pages | 119-30 |
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Authors | Holzl H, Kapelari B, Kellermann J, Seemuller E, Sumegi M, Udvardy A, Medalia O, Sperling J, Muller SA, Engel A, Baumeister W |
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Title | The regulatory complex of Drosophila melanogaster 26S proteasomes. Subunit composition and localization of a deubiquitylating enzyme. |
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[11] |
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PubMed ID | 11390388 |
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Journal | J Biol Chem |
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Year | 2001 |
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Volume | 276 |
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Pages | 30366-73 |
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Authors | Mullally JE, Moos PJ, Edes K, Fitzpatrick FA |
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Title | Cyclopentenone prostaglandins of the J series inhibit the ubiquitin isopeptidase activity of the proteasome pathway. |
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[12] |
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PubMed ID | 12705903 |
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Journal | Biochem Biophys Res Commun |
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Year | 2003 |
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Volume | 304 |
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Pages | 176-83 |
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Authors | Nishikawa K, Li H, Kawamura R, Osaka H, Wang YL, Hara Y, Hirokawa T, Manago Y, Amano T, Noda M, Aoki S, Wada K |
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Title | Alterations of structure and hydrolase activity of parkinsonism-associated human ubiquitin carboxyl-terminal hydrolase L1 variants. |
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[13] |
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PubMed ID | 15571815 |
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Journal | Biochim Biophys Acta |
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Year | 2004 |
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Volume | 1695 |
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Pages | 189-207 |
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Authors | Amerik AY, Hochstrasser M |
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Title | Mechanism and function of deubiquitinating enzymes. |
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[14] |
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Comments | X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) IN COMPLEX WITH UBIQUITIN VINYLMETHYLESTER, AND ENZYMATIC ACTIVITY. |
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PubMed ID | 15531586 |
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Journal | J Biol Chem |
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Year | 2005 |
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Volume | 280 |
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Pages | 1512-20 |
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Authors | Misaghi S, Galardy PJ, Meester WJ, Ovaa H, Ploegh HL, Gaudet R |
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Title | Structure of the ubiquitin hydrolase UCH-L3 complexed with a suicide substrate. |
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Related PDB | 1xd3 |
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Related UniProtKB | P15374 |
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comments | This enzyme belongs to the peptidase family-C12. According to the literature & Swissprot data, this enzyme catalyzes hydrolyses of amide bond (including peptide bond), thioester bond, and carboxlic ester bond. According to the literature [4] & [8], this enzyme has got a catalytic triad composed of Cys/His/Asp and an oxyanion hole, made up by mainchain amide of the cysteine residue and sidechain amide of Gln. The catalytic mechanism is also similar to other cysteine proteases, in which cysteine acts as a nucleophile, and histidine acts as a general acid-base.
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created | updated |
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2005-07-22 | 2012-10-23 |
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