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Tyrosinemias
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D020176 |
[A group of disorders which have in common elevations of tyrosine in the blood and urine secondary to an enzyme deficiency. Type I tyrosinemia features episodic weakness, self-mutilation, hepatic necrosis, renal tubular injury, and seizures and is caused by a deficiency of the enzyme fumarylacetoacetase. Type II tyrosinemia features INTELLECTUAL DISABILITY, painful corneal ulcers, and keratoses of the palms and plantar surfaces and is caused by a deficiency of the enzyme TYROSINE TRANSAMINASE. Type III tyrosinemia features INTELLECTUAL DISABILITY and is caused by a deficiency of the enzyme 4-HYDROXYPHENYLPYRUVATE DIOXYGENASE. (Menkes, Textbook of Child Neurology, 5th ed, pp42-3)
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Tyrothricin
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D014449 |
[A polypeptide antibiotic mixture obtained from Bacillus brevis. It consists of a mixture of three tyrocidines (60%) and several gramicidins (20%) and is very toxic to blood, liver, kidneys, meninges, and the olfactory apparatus. It is used topically.
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Tyrphostins
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D020032 |
[A family of synthetic protein tyrosine kinase inhibitors. They selectively inhibit receptor autophosphorylation and are used to study receptor function.
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U937 Cells
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D020298 |
[A human cell line established from a diffuse histiocytic lymphoma (HISTIOCYTIC LYMPHOMA, DIFFUSE) and displaying many monocytic characteristics. It serves as an in vitro model for MONOCYTE and MACROPHAGE differentiation.
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UDPglucose 4-Epimerase
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D014534 |
[A necessary enzyme in the metabolism of galactose. It reversibly catalyzes the conversion of UDPglucose to UDPgalactose. NAD+ is an essential component for enzymatic activity. EC 5.1.3.2.
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UDPglucose-Hexose-1-Phosphate Uridylyltransferase
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D006599 |
[An enzyme that catalyzes the transfer of UMP from UDPglucose to galactose 1-phosphate, forming UDPgalactose and glucose 1-phosphate. Deficiency in this enzyme is the major cause of GALACTOSEMIA. EC 2.7.7.12.
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UNESCO
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D000076892 |
[An operating body of the UNITED NATIONS, responsible for coordinating international cooperation in education, science, culture and communication.
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USSR
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D014586 |
[A country located from the Baltic and Black seas to the Pacific Ocean and, for a time including 15 Soviet Socialist Republics. The capital was Moscow.
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UTP-Glucose-1-Phosphate Uridylyltransferase
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D005957 |
[An enzyme that catalyzes the formation of UDPglucose from UTP plus glucose 1-phosphate. EC 2.7.7.9.
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UTP-Hexose-1-Phosphate Uridylyltransferase
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D005694 |
[An enzyme that catalyzes the synthesis of UDPgalactose from UTP and galactose-1-phosphate. It is present in low levels in fetal and infant liver, but increases with age, thereby enabling galactosemic infants who survive to develop the capacity to metabolize galactose. EC 2.7.7.10.
] |
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Ubiquinone
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D014451 |
[A lipid-soluble benzoquinone which is involved in ELECTRON TRANSPORT in mitochondrial preparations. The compound occurs in the majority of aerobic organisms, from bacteria to higher plants and animals.
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Ubiquitin
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D025801 |
[A highly conserved 76-amino acid peptide universally found in eukaryotic cells that functions as a marker for intracellular PROTEIN TRANSPORT and degradation. Ubiquitin becomes activated through a series of complicated steps and forms an isopeptide bond to lysine residues of specific proteins within the cell. These "ubiquitinated" proteins can be recognized and degraded by proteosomes or be transported to specific compartments within the cell.
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Ubiquitin C
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D025822 |
[A single protein comprised of tandem repeats of the UBIQUITIN 78-amino acid sequence. It is a product of the polyubiquitin gene which contains multiple copies of the ubiquitin coding sequence. Proteolytic processing of ubiquitin C results in the formation of individual ubiquitin molecules. This protein is distinct from POLYUBIQUITIN, which is a protein formed through isopeptide linkage of multiple ubiquitin species.
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Ubiquitin Thiolesterase
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D043222 |
[A thioester hydrolase which acts on esters formed between thiols such as DITHIOTHREITOL or GLUTATHIONE and the C-terminal glycine residue of UBIQUITIN.
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Ubiquitin-Activating Enzymes
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D044764 |
[A class of enzymes that catalyzes the ATP-dependent formation of a thioester bond between itself and UBIQUITIN. It then transfers the activated ubiquitin to one of the UBIQUITIN-PROTEIN LIGASES.
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Ubiquitin-Conjugating Enzymes
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D044763 |
[A class of enzymes that form a thioester bond to UBIQUITIN with the assistance of UBIQUITIN-ACTIVATING ENZYMES. They transfer ubiquitin to the LYSINE of a substrate protein with the assistance of UBIQUITIN-PROTEIN LIGASES.
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Ubiquitin-Protein Ligase Complexes
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D043743 |
[Complexes of enzymes that catalyze the covalent attachment of UBIQUITIN to other proteins by forming a peptide bond between the C-terminal GLYCINE of UBIQUITIN and the alpha-amino groups of LYSINE residues in the protein. The complexes play an important role in mediating the selective-degradation of short-lived and abnormal proteins. The complex of enzymes can be broken down into three components that involve activation of ubiquitin (UBIQUITIN-ACTIVATING ENZYMES), conjugation of ubiquitin to the ligase complex (UBIQUITIN-CONJUGATING ENZYMES), and ligation of ubiquitin to the substrate protein (UBIQUITIN-PROTEIN LIGASES).
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Ubiquitin-Protein Ligases
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D044767 |
[A diverse class of enzymes that interact with UBIQUITIN-CONJUGATING ENZYMES and ubiquitination-specific protein substrates. Each member of this enzyme group has its own distinct specificity for a substrate and ubiquitin-conjugating enzyme. Ubiquitin-protein ligases exist as both monomeric proteins multiprotein complexes.
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Ubiquitin-Specific Peptidase 7
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D000076084 |
[A ubiquitinyl hydrolase that deubiquitinates several proteins with critical roles in DNA REPAIR, cell growth, and survival, including TUMOR SUPPRESSOR PROTEIN P53; MDM-2 PROTEIN; and PTEN PHOSPHOHYDROLASE. It also stabilizes herpesvirus 1 trans-acting transcriptional protein VMW110 during HSV-1 infection, contributing to its function as a TRANS-ACTIVATOR.
] |
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Ubiquitin-Specific Proteases
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D064570 |
[Members of the peptidase C19 family which regulate signal transduction by removing UBIQUITIN from specific protein substrates via a process known as deubiquitination or deubiquitylation.
] |