An enzyme that catalyzes the conversion of L-TYROSINE and 2-oxoglutarate to 4-hydroxyphenylpyruvate and L-GLUTAMATE. It is a pyridoxal-phosphate protein. L-PHENYLALANINE is hydroxylated to L-tyrosine. The mitochondrial enzyme may be identical with ASPARTATE AMINOTRANSFERASES (EC 2.6.1.1.). Deficiency of this enzyme may cause type II Tyrosinemia (see TYROSINEMIAS). EC 2.6.1.5.
Any operation on the spinal cord. (Stedman, 26th ed)
A non-essential amino acid. In animals it is synthesized from PHENYLALANINE. It is also the precursor of EPINEPHRINE; THYROID HORMONES; and melanin.
An enzyme that catalyzes the conversion of L-alanine and 2-oxoglutarate to pyruvate and L-glutamate. (From Enzyme Nomenclature, 1992) EC 2.6.1.2.
An enzyme that converts brain gamma-aminobutyric acid (GAMMA-AMINOBUTYRIC ACID) into succinate semialdehyde, which can be converted to succinic acid and enter the citric acid cycle. It also acts on beta-alanine. EC 2.6.1.19.
A subclass of enzymes of the transferase class that catalyze the transfer of an amino group from a donor (generally an amino acid) to an acceptor (generally a 2-keto acid). Most of these enzymes are pyridoxyl phosphate proteins. (Dorland, 28th ed) EC 2.6.1.
Enzymes of the transferase class that catalyze the conversion of L-aspartate and 2-ketoglutarate to oxaloacetate and L-glutamate. EC 2.6.1.1.
A PYRIDOXAL PHOSPHATE containing enzyme that catalyzes the reversible transfer of an amino group between D-Alanine and alpha-ketoglutarate to form PYRUVATE and D-GLUTAMATE, respectively. It plays a role in the synthesis of the bacterial CELL WALL. This enzyme was formerly classified as EC 2.6.1.10.

Tyrosine aminotransferase catalyzes the final step of methionine recycling in Klebsiella pneumoniae. (1/329)

An aminotransferase which catalyzes the final step in methionine recycling from methylthioadenosine, the conversion of alpha-ketomethiobutyrate to methionine, has been purified from Klebsiella pneumoniae and characterized. The enzyme was found to be a homodimer of 45-kDa subunits, and it catalyzed methionine formation primarily using aromatic amino acids and glutamate as the amino donors. Histidine, leucine, asparagine, and arginine were also functional amino donors but to a lesser extent. The N-terminal amino acid sequence of the enzyme was determined and found to be almost identical to the N-terminal sequence of both the Escherichia coli and Salmonella typhimurium tyrosine aminotransferases (tyrB gene products). The structural gene for the tyrosine aminotransferase was cloned from K. pneumoniae and expressed in E. coli. The deduced amino acid sequence displayed 83, 80, 38, and 34% identity to the tyrosine aminotransferases from E. coli, S. typhimurium, Paracoccus denitrificans, and Rhizobium meliloti, respectively, but it showed less than 13% identity to any characterized eukaryotic tyrosine aminotransferase. Structural motifs around key invariant residues placed the K. pneumoniae enzyme within the Ia subfamily of aminotransferases. Kinetic analysis of the aminotransferase showed that reactions of an aromatic amino acid with alpha-ketomethiobutyrate and of glutamate with alpha-ketomethiobutyrate proceed as favorably as the well-known reactions of tyrosine with alpha-ketoglutarate and tyrosine with oxaloacetate normally associated with tyrosine aminotransferases. The aminotransferase was inhibited by the aminooxy compounds canaline and carboxymethoxylamine but not by substrate analogues, such as nitrotyrosine or nitrophenylalanine.  (+info)

Synthesis of a liver enzyme in hybrid cells. (2/329)

Rat hepatoma cells were fused with cells of an established mouse lymphoma line, with normal diploid mouse macrophages, lymphocytes and fibroblasts and with normal diploid rat macrophages and lymphocytes. The liver-specific enzyme tyrosine aminotransferase was produced by almost all the hybrid cells, but usually at a lower level than in the parental hepatoma cells. Most of the hybrids also showed increased levels of this enzyme after exposure to dexamethasone. In the rat x mouse hybrids, the electrophoretic mobility of the enzyme indicated that only the rat hepatoma enzyme was produced. The findings are difficult to explain in terms of simple models involving a single diffusible repressor or activator of tyrosine aminotransferase synthesis.  (+info)

Two new members of the emerging KDWK family of combinatorial transcription modulators bind as a heterodimer to flexibly spaced PuCGPy half-sites. (3/329)

Initially recognized as a HeLa factor essential for parvovirus DNA replication, parvovirus initiation factor (PIF) is a site-specific DNA-binding complex consisting of p96 and p79 subunits. We have cloned and sequenced the human cDNAs encoding each subunit and characterized their products expressed from recombinant baculoviruses. The p96 and p79 polypeptides have 40% amino acid identity, focused particularly within a 94-residue region containing the sequence KDWK. This motif, first described for the Drosophila homeobox activator DEAF-1, identifies an emerging group of metazoan transcriptional modulators. During viral replication, PIF critically regulates the viral nickase, but in the host cell it probably modulates transcription, since each subunit is active in promoter activation assays and the complex binds to previously described regulatory elements in the tyrosine aminotransferase and transferrin receptor promoters. Within its recognition site, PIF binds coordinately to two copies of the tetranucleotide PuCGPy, which, remarkably, can be spaced from 1 to 15 nucleotides apart, a novel flexibility that we suggest may be characteristic of the KDWK family. Such tetranucleotides are common in promoter regions, particularly in activating transcription factor/cyclic AMP response element-binding protein (ATF/CREB) and E-box motifs, suggesting that PIF may modulate the transcription of many genes.  (+info)

Crystal structure of Trypanosoma cruzi tyrosine aminotransferase: substrate specificity is influenced by cofactor binding mode. (4/329)

The crystal structure of tyrosine aminotransferase (TAT) from the parasitic protozoan Trypanosoma cruzi, which belongs to the aminotransferase subfamily Igamma, has been determined at 2.5 A resolution with the R-value R = 15.1%. T. cruzi TAT shares less than 15% sequence identity with aminotransferases of subfamily Ialpha but shows only two larger topological differences to the aspartate aminotransferases (AspATs). First, TAT contains a loop protruding from the enzyme surface in the larger cofactor-binding domain, where the AspATs have a kinked alpha-helix. Second, in the smaller substrate-binding domain, TAT has a four-stranded antiparallel beta-sheet instead of the two-stranded beta-sheet in the AspATs. The position of the aromatic ring of the pyridoxal-5'-phosphate cofactor is very similar to the AspATs but the phosphate group, in contrast, is closer to the substrate-binding site with one of its oxygen atoms pointing toward the substrate. Differences in substrate specificities of T. cruzi TAT and subfamily Ialpha aminotransferases can be attributed by modeling of substrate complexes mainly to this different position of the cofactor-phosphate group. Absence of the arginine, which in the AspATs fixes the substrate side-chain carboxylate group by a salt bridge, contributes to the inability of T. cruzi TAT to transaminate acidic amino acids. The preference of TAT for tyrosine is probably related to the ability of Asn17 in TAT to form a hydrogen bond to the tyrosine side-chain hydroxyl group.  (+info)

Physical and genetic mapping of the macular corneal dystrophy locus on chromosome 16q and exclusion of TAT and LCAT as candidate genes. (5/329)

PURPOSE: Macular corneal dystrophy (MCD) is an inherited autosomal recessive disorder that has been subdivided into three immunophenotypes, MCD types I, IA and II. We previously mapped the MCD type I gene to chromosome 16q22 and suggested that the MCD type II gene was linked to the same region. The purpose of this study was to construct a genomic contig spanning the MCD region and to narrow the MCD critical interval by haplotype analysis. The TAT and LCAT genes were mapped to determine if they might be the MCD gene. METHODS: The MCD contig was constructed by screening YAC, PAC, and BAC libraries with microsatellite, STS and EST markers, employing a systematic "DNA walking" technique. Polymorphic markers mapped and ordered on the contig were used to screen the MCD affected individuals and their family members for haplotype analysis. RESULTS: Twenty-two YAC, 30 PAC, and 17 BAC clones were mapped to form the MCD contig. Markers mapped on the contig include 19 microsatellite, 14 STS, and 15 EST markers. Moreover, 18 novel STS markers were generated. Using the mapped and ordered microsatellite markers, haplotype analysis on 21 individuals with MCD type I or type II and their family members from Iceland narrowed the MCD interval to 3 overlapping PAC clones. In addition, the TAT and LCAT genes were mapped outside the MCD region. CONCLUSIONS: We established a genomic contig for the MCD region and dramatically narrowed the MCD critical interval. Mapping data show that the TAT and LCAT genes are not the cause of MCD.  (+info)

Evidence for a common step in three different processes for modulating the kinetic properties of glucocorticoid receptor-induced gene transcription. (6/329)

The dose-response curve of steroid hormones and the associated EC(50) value are critical parameters both in the development of new pharmacologically active compounds and in the endocrine therapy of various disease states. We have recently described three different variables that can reposition the dose-response curve of agonist-bound glucocorticoid receptors (GRs): a 21-base pair sequence of the rat tyrosine aminotransferase gene called a glucocorticoid modulatory element (GME), GR concentration, and coactivator concentration. At the same time, each of these three components was found to influence the partial agonist activity of antiglucocorticoids. In an effort to determine whether these three processes proceed via independent pathways or a common intermediate, we have examined several mechanistic details. The effects of increasing concentrations of both GR and the coactivator TIF2 are found to be saturable. Furthermore, saturating levels of either GR or TIF2 inhibit the ability of each protein, and the GME, to affect further changes in the dose-response curve or partial agonist activity of antisteroids. This competitive inhibition suggests that all three modulators proceed through a common step involving a titratable factor. Support for this hypothesis comes from the observation that a fragment of the coactivator TIF2 retaining intrinsic transactivation activity is a dominant negative inhibitor of each component (GME, GR, and coactivator). This inhibition was not due to nonspecific effects on the general transcription machinery as the VP16 transactivation domain was inactive. The viral protein E1A also prevented the action of each of the three components in a manner that was independent of E1A's ability to block the histone acetyltransferase activity of CBP. Collectively, these results suggest that three different inputs (GME, GR, and coactivator) for perturbing the dose-response curve, and partial agonist activity, of GR-steroid complexes act by converging at a single step that involves a limiting factor prior to transcription initiation.  (+info)

Temporal analysis of hepatocyte differentiation by small hepatocyte-like progenitor cells during liver regeneration in retrorsine-exposed rats. (7/329)

Liver regeneration after two-thirds surgical partial hepatectomy (PH) in rats treated with the pyrrolizidine alkaloid retrorsine is accomplished through the activation, expansion, and differentiation of a population of small hepatocyte-like progenitor cells (SHPCs). We have examined expression of the major liver-enriched transcription factors, cytochrome P450 (CYP) enzymes, and other markers of hepatocytic differentiation in SHPCs during the protracted period of liver regeneration after PH in retrorsine-exposed rats. Early-appearing SHPCs (at 3-7 days after PH) express mRNAs for all of the major liver-enriched transcription factors at varying levels compared to fully differentiated hepatocytes. In addition, SHPCs lack (or have significantly reduced) expression of mRNA for hepatocyte markers tyrosine aminotransferase and alpha-1 antitrypsin, but their expression levels of mRNA and/or protein for WT1 and alpha-fetoprotein (AFP) are increased. With the exception of AFP expression, SHPCs resembled fully differentiated hepatocytes by 14 days after PH. Expression of AFP was maintained by most SHPCs through 14 days after PH, gradually declined through 23 days after PH, and was essentially absent from SHPC progeny by 30 days after PH. Furthermore, early appearing SHPCs lack (or have reduced expression) of hepatic CYP proteins known to be induced in rat livers after retrorsine exposure. The resistance of SHPCs to the mitoinhibitory effects of retrorsine may be directly related to a lack of CYP enzymes required to metabolize retrorsine to its toxic derivatives. These results suggest that SHPCs represent a unique parenchymal (less differentiated) progenitor cell population of adult rodent liver that is phenotypically distinct from fully differentiated hepatocytes, biliary epithelial cells, and (ductular) oval cells.  (+info)

Rat liver tryptophan pyrrolase activity and gene expression during alcohol withdrawal. (8/329)

Rat liver tryptophan (Trp) pyrrolase activity and gene expression were studied in relation to the alcohol-withdrawal syndrome (AWS). Both activity and gene expression were enhanced after withdrawal of ethanol-containing liquid diets and the time-course of these changes mirrored that of development and intensity of the behavioural disturbances of the AWS. By contrast, no correlation was observed between the AWS-induced behaviour and changes in activity of another hepatic glucocorticoid-inducible enzyme, tyrosine aminotransferase, and a negative correlation was noted between behaviour and the gene expression of this latter enzyme and also of that of the hepatic glucocorticoid receptor. We suggest that the metabolic consequences of activation of liver Trp pyrrolase during alcohol withdrawal may play a role in the behavioural features of the AWS.  (+info)

Tyrosine transaminase, also known as tyrosine aminotransferase or TAT, is an enzyme that plays a crucial role in the metabolism of the amino acid tyrosine. This enzyme catalyzes the transfer of an amino group from tyrosine to a ketoacid, such as alpha-ketoglutarate, resulting in the formation of a new amino acid, glutamate, and a ketone derivative of tyrosine.

Tyrosine transaminase is primarily found in the liver and its activity can be used as a biomarker for liver function. Increased levels of this enzyme in the blood may indicate liver damage or disease, such as hepatitis or cirrhosis. Therefore, measuring tyrosine transaminase activity is often part of routine liver function tests.

Cordotomy is a surgical procedure that involves selectively cutting the spinothalamic tract, which carries pain and temperature signals from the body to the brain. This procedure is typically performed in the cervical (neck) region of the spinal cord and is used to treat chronic, severe pain that has not responded to other forms of treatment.

During a cordotomy, a neurosurgeon uses a specialized needle or electrode to locate and destroy the specific nerve fibers responsible for transmitting painful sensations from a particular part of the body. The procedure can be performed under local anesthesia with sedation or general anesthesia, depending on the patient's preferences and medical condition.

While cordotomy can provide significant pain relief in the short term, it is not a permanent solution, as the nerve fibers may eventually regenerate over time. Additionally, there are risks associated with the procedure, including weakness or numbness in the affected limbs, difficulty swallowing, and in rare cases, respiratory failure. Therefore, cordotomy is typically reserved for patients with severe pain who have exhausted other treatment options and have a limited life expectancy due to their underlying medical condition.

Tyrosine is an non-essential amino acid, which means that it can be synthesized by the human body from another amino acid called phenylalanine. Its name is derived from the Greek word "tyros," which means cheese, as it was first isolated from casein, a protein found in cheese.

Tyrosine plays a crucial role in the production of several important substances in the body, including neurotransmitters such as dopamine, norepinephrine, and epinephrine, which are involved in various physiological processes, including mood regulation, stress response, and cognitive functions. It also serves as a precursor to melanin, the pigment responsible for skin, hair, and eye color.

In addition, tyrosine is involved in the structure of proteins and is essential for normal growth and development. Some individuals may require tyrosine supplementation if they have a genetic disorder that affects tyrosine metabolism or if they are phenylketonurics (PKU), who cannot metabolize phenylalanine, which can lead to elevated tyrosine levels in the blood. However, it is important to consult with a healthcare professional before starting any supplementation regimen.

Alanine transaminase (ALT) is a type of enzyme found primarily in the cells of the liver and, to a lesser extent, in the cells of other tissues such as the heart, muscles, and kidneys. Its primary function is to catalyze the reversible transfer of an amino group from alanine to another alpha-keto acid, usually pyruvate, to form pyruvate and another amino acid, usually glutamate. This process is known as the transamination reaction.

When liver cells are damaged or destroyed due to various reasons such as hepatitis, alcohol abuse, nonalcoholic fatty liver disease, or drug-induced liver injury, ALT is released into the bloodstream. Therefore, measuring the level of ALT in the blood is a useful diagnostic tool for evaluating liver function and detecting liver damage. Normal ALT levels vary depending on the laboratory, but typically range from 7 to 56 units per liter (U/L) for men and 6 to 45 U/L for women. Elevated ALT levels may indicate liver injury or disease, although other factors such as muscle damage or heart disease can also cause elevations in ALT.

4-Aminobutyrate transaminase (GABA transaminase or GABA-T) is an enzyme that catalyzes the reversible transfer of an amino group from 4-aminobutyrate (GABA) to 2-oxoglutarate, forming succinic semialdehyde and glutamate. This enzyme plays a crucial role in the metabolism of the major inhibitory neurotransmitter gamma-aminobutyric acid (GABA) in the central nervous system. Inhibition of GABA transaminase is a therapeutic strategy for the treatment of various neurological disorders, such as epilepsy and anxiety, due to its ability to increase GABA levels in the brain.

Transaminases, also known as aminotransferases, are a group of enzymes found in various tissues of the body, particularly in the liver, heart, muscle, and kidneys. They play a crucial role in the metabolism of amino acids, the building blocks of proteins.

There are two major types of transaminases: aspartate aminotransferase (AST) and alanine aminotransferase (ALT). Both enzymes are normally present in low concentrations in the bloodstream. However, when tissues that contain these enzymes are damaged or injured, such as during liver disease or muscle damage, the levels of AST and ALT in the blood may significantly increase.

Measurement of serum transaminase levels is a common laboratory test used to assess liver function and detect liver injury or damage. Increased levels of these enzymes in the blood can indicate conditions such as hepatitis, liver cirrhosis, drug-induced liver injury, heart attack, and muscle disorders. It's important to note that while elevated transaminase levels may suggest liver disease, they do not specify the type or cause of the condition, and further diagnostic tests are often required for accurate diagnosis and treatment.

Aspartate aminotransferases (ASTs) are a group of enzymes found in various tissues throughout the body, including the heart, liver, and muscles. They play a crucial role in the metabolic process of transferring amino groups between different molecules.

In medical terms, AST is often used as a blood test to measure the level of this enzyme in the serum. Elevated levels of AST can indicate damage or injury to tissues that contain this enzyme, such as the liver or heart. For example, liver disease, including hepatitis and cirrhosis, can cause elevated AST levels due to damage to liver cells. Similarly, heart attacks can also result in increased AST levels due to damage to heart muscle tissue.

It is important to note that an AST test alone cannot diagnose a specific medical condition, but it can provide valuable information when used in conjunction with other diagnostic tests and clinical evaluation.

D-Alanine transaminase (DAT or Dalat) is an enzyme that catalyzes the reversible transfer of an amino group from D-alanine to α-ketoglutarate, producing pyruvate and D-glutamate. It is found in various bacteria and plays a role in their metabolism. However, it is not typically considered a medically significant enzyme in humans, as it is not commonly used as a clinical marker of liver or other organ function.

... (or tyrosine transaminase) is an enzyme present in the liver and catalyzes the conversion of tyrosine ... Dietrich JB (April 1992). "Tyrosine aminotransferase: a transaminase among others?". Cellular and Molecular Biology. 38 (2): 95 ... L-tyrosine + 2-oxoglutarate ⇌ {\displaystyle \rightleftharpoons } 4-hydroxyphenylpyruvate + L-glutamate In humans, the tyrosine ... and elevated blood tyrosine levels. Keratitis in Tyrosinemia type II patients is caused by the deposition of tyrosine crystals ...
Nakano M (January 1967). "Purification and properties of halogenated tyrosine and thyroid hormone transaminase from rat kidney ... and halogenated tyrosine transaminase. It employs one cofactor, pyridoxal phosphate. ... The systematic name of this enzyme class is 3,5-diiodo-L-tyrosine:2-oxoglutarate aminotransferase. Other names in common use ... In enzymology, a diiodotyrosine transaminase (EC 2.6.1.24) is an enzyme that catalyzes the chemical reaction 3,5-diiodo-L- ...
para-hydroxyphenylalanine) begins with an α-ketoglutarate dependent transamination through the tyrosine transaminase to para- ... It transforms L-tyrosine into p-coumaric acid.Tyrosine is also the precursor to the pigment melanin. Tyrosine (or its precursor ... Tyrosine residues may also be modified by the addition of a sulfate group, a process known as tyrosine sulfation. Tyrosine ... Tyrosine MS Spectrum Tyrosine metabolism Archived 2019-07-26 at the Wayback Machine Phenylalanine and tyrosine biosynthesis ...
... tyrosine transaminase deficiency, systemic lysosomal storage diseases, and several skin diseases (X-linked ichthyosis, ...
... alanine transaminase EC 2.6.1.3: cysteine transaminase EC 2.6.1.4: glycine transaminase EC 2.6.1.5: tyrosine transaminase EC ... D-amino-acid transaminase EC 2.6.1.11: acetylornithine transaminase EC 2.6.1.12: alanine-oxo-acid transaminase EC 2.6.1.13: ... neamine transaminase EC 2.6.1.94: 2′-deamino-2′-hydroxyneamine transaminase EC 2.6.1.95: neomycin C transaminase EC 2.6.1.96: 4 ... UDP-N-acetylbacillosamine transaminase EC 2.6.1.35: glycine-oxaloacetate transaminase EC 2.6.1.36: L-lysine 6-transaminase EC ...
In the case of aspartate transaminase, which can act on tyrosine, phenylalanine, and tryptophan, it reversibly transfers an ... This includes enzymes like transaminase (also known as "aminotransferase"), and a very small number of oximinotransferases and ... "transaminase"), was first noted in 1930 by Dorothy M. Needham, after observing the disappearance of glutamic acid added to ...
... phenylalanine-DOPP transaminase (PDT), DOPA 2-oxoglutarate aminotransferase, and DOPAATS. This enzyme participates in tyrosine ... aspartate-DOPP transaminase (ADT), L-dopa transaminase, dopa aminotransferase, glutamate-DOPP transaminase (GDT), ... In enzymology, a dihydroxyphenylalanine transaminase (EC 2.6.1.49) is an enzyme that catalyzes the chemical reaction 3,4- ... This enzyme belongs to the family of transferases, specifically the transaminases, which transfer nitrogenous groups. The ...
Heilbronn J, Wilson J, Berger BJ (March 1999). "Tyrosine aminotransferase catalyzes the final step of methionine recycling in ... Methionine transaminase (EC 2.6.1.88, methionine-oxo-acid transaminase) is an enzyme with systematic name L-methionine:2-oxo- ... Methionine+transaminase at the U.S. National Library of Medicine Medical Subject Headings (MeSH) Portal: Biology (EC 2.6.1). ...
This enzyme participates in 5 metabolic pathways: histidine metabolism, tyrosine metabolism, phenylalanine metabolism, ... Other names in common use include imidazolylacetolphosphate transaminase, glutamic-imidazoleacetol phosphate transaminase, ... imidazoleacetol phosphate transaminase, IAP transaminase, and imidazolylacetolphosphate aminotransferase. ... In enzymology, a histidinol-phosphate transaminase (EC 2.6.1.9) is an enzyme that catalyzes the chemical reaction L-histidinol ...
This enzyme participates in 6 metabolic pathways: methionine metabolism, tyrosine metabolism, phenylalanine metabolism, ... In enzymology, an aromatic-amino-acid transaminase (EC 2.6.1.57) is an enzyme that catalyzes the chemical reaction an aromatic ... This enzyme belongs to the family of transferases, specifically the transaminases, which transfer nitrogenous groups. The ... phenylalanine, tyrosine and tryptophan biosynthesis, novobiocin biosynthesis, and alkaloid biosynthesis i. It employs one ...
In these animals, tyrosine is synthesized from phenylalanine via the enzyme phenylalanine hydroxylase, whereas plants have ... In enzymology, glutamate-prephenate aminotransferase (EC 2.6.1.79, also known as prephenate transaminase, PAT, and L-glutamate: ... This is a necessary process for any organism which needs to convert arogenate into phenylalanine or tyrosine, as arogenate is ... It operates in the phenylalanine and tyrosine biosynthesis pathway. The gene which encodes this enzyme has recently been ...
... in particular tyrosine. Tyrosine is a conditionally essential amino acid for PKU patients because without PAH it cannot be ... Excessive phenylalanine can be metabolized into phenylketones through the minor route, a transaminase pathway with glutamate. ... Tyrosine, which is normally derived from phenylalanine and which is necessary for normal brain function, is usually ... Tetrahydrobiopterin is required to convert Phe to Tyr and is required to convert Tyr to L-DOPA via the enzyme tyrosine ...
... adds and removes tyrosine residues on α-tubulin), GOT1 (an Aspartate transaminase), and ACSL6 (a Long-chain-fatty-acid-CoA ... It is proposed that tyrosine kinase inhibitors with specificity for NTRK3's tyrosine kinase activity in ETV6-NTRK3 gene- ... The table includes abbreviations for tyrosine kinase receptor (TK receptor), non-receptor tyrosine kinase (non-receptor TK), ... the ETV6 gene fusion to receptor tyrosine kinases and non-receptor tyrosine kinases may be sensitive to therapy with tyrosine ...
Tyrosine, a similar amino acid, differs by a methylene group (CH2) between the aromatic ring and the alpha carbon. HPG is ... Finally, 4-hydroxyphenylglycine transaminase (HpgT) transfers an ammonia moiety from a donor to 4-hydroxylbenzoylformate to ... Several different molecules can serve as the nitrogen donor for the transamination, however, Hubbard et al suspect L-tyrosine ... synthesized from prephenate, an intermediate in the shikimic acid pathway and also a precursor to tyrosine. Prephenate is ...
BIBW 2992 is a next-generation tyrosine kinase inhibitor developed by Boehringer Ingelheim which irreversibly blocks both ... BIBW 2992 was well tolerated, with reversible adverse events including rash, diarrhoea, elevations in transaminases. BIBW 2992 ... tyrosine kinase in a 2-week on, 2-week off schedule in patients with advanced solid tumours". British Journal of Cancer. 98 (1 ... by targeting receptor tyrosine kinases. Examples include nintedanib (BIBF 1120), afatinib (BIBW 2992) and motesanib (AMG 706). ...
... tryptophan transaminase MeSH D08.811.913.477.700.900 - tyrosine transaminase MeSH D08.811.913.555.150 - amidinotransferases ... glycine transaminase MeSH D08.811.913.477.700.535 - leucine transaminase MeSH D08.811.913.477.700.550 - l-lysine 6-transaminase ... transaminases MeSH D08.811.913.477.700.100 - alanine transaminase MeSH D08.811.913.477.700.120 - 2-aminoadipate transaminase ... receptor protein-tyrosine kinases MeSH D08.811.913.696.620.682.725.400.020 - fms-like tyrosine kinase 3 MeSH D08.811.913.696. ...
The group studies deficiencies in aromatic amino acid decarboxylase, tyrosine hydroxylase, dopamine beta-hydroxylase, monoamine ... GABA-transaminase, and succinate-semialdehyde dehydroxylase. Opladen, T.; Cortes-Saladelafont, E.; Mastrangelo, M.; Horvath, G ...
Likewise, lysine, tyrosine and cysteine will typically act as a Brønsted acid. Histidine under these conditions can act both as ... This process involves transaminases, often the same as those used in amination during synthesis. In many vertebrates, the amino ... The oxidation pathway starts with the removal of the amino group by a transaminase; the amino group is then fed into the urea ... None of these amino acids' side chains ionize easily, and therefore do not have pKas, with the exception of tyrosine (Tyr, Y). ...
Enzymes called transaminases can easily transfer the amino group from one amino acid (making it an α-keto acid) to another α- ... and tyrosine, the nonessential amino acids. While they can synthesize arginine and histidine, they cannot produce it in ...
... transaminase Dème D, Fimiani E, Pommier J, Nunez J (February 1975). "Free diiodotyrosine effects on protein ... Iodinated tyrosine derivatives, All stub articles, Organohalide stubs). ...
It is a small molecule inhibitor of the tyrosine kinases c-Met and VEGFR2, and also inhibits AXL and RET. It was discovered and ... elevated transaminases, higher cholesterol levels, and loss of red and white blood cells. Common adverse effects (between 1% ... Cabozantinib inhibits the following receptor tyrosine kinases: MET (hepatocyte growth factor receptor protein) and VEGFR, RET, ... GAS6 receptor (AXL), KIT), and Fms-like tyrosine kinase-3 (FLT3). Cabozantinib was granted orphan drug status by the US Food ...
Many proteins become tyrosine phosphorylated in response to CSF1R signaling (Table 1) including p85, Cbl, and Gab3 which are ... alanine transaminase), edema, nausea, lacrimation, and reduced appetite, but no signs of liver toxicity were found. There are ... CSF1R, the protein encoded by the CSF1R gene is a tyrosine kinase transmembrane receptor and member of the CSF1/PDGF receptor ... The cytoplasmic domain has a juxtamembrane domain and tyrosine kinase domain that is interrupted by a kinase insert domain. At ...
Tyrosine can also be inhibited at the transcriptional level by the TyrR repressor. TyrR binds to the TyrR boxes on the operon ... The genes that encode both the dihydroxy acid dehydrase used in the creation of α-ketoisovalerate and Transaminase E, as well ... Tyrosine and phenylalanine are biosynthesized from prephenate, which is converted to an amino acid-specific intermediate. This ... Phenylalanine, tyrosine, and tryptophan, the aromatic amino acids, arise from chorismate. The first step, condensation of 3- ...
An example of a commonly evolved enzyme is ω-transaminase which can replace a ketone with a chiral amine and consequently ... Protein tyrosine phospatase(PTP) and human carbonic anhydrase II (CAII)) has shown the main activity is "robust" towards change ... Shin JS, Kim BG (August 2001). "Comparison of the omega-transaminases from different microorganisms and application to ... whereas the next most catalysed native amino acid was the structurally similar tyrosine, but at a thousandth as much as ...
Laboratory abnormalities have included alanine transaminase (ALT) abnormalities, aspartate transaminase (AST) abnormalities, ... Clinical trial number NCT03610971 for "Treatment Free Remission After Combination Therapy With Ruxolitinib Plus Tyrosine Kinase ... Non-receptor tyrosine kinase inhibitors, Pyrrolopyrimidines, Pyrazoles, Nitriles, Cyclopentanes, Novartis brands, Orphan drugs) ... "Treatment Free Remission After Combination Therapy With Ruxolitinib Plus Tyrosine Kinase Inhibitors".[full citation needed][ ...
... protein tyrosine phosphatase, non-receptor type 11 (Noonan syndrome 1) PUS1: encoding enzyme tRNA pseudouridine synthase A ... encoding protein Branched chain amino acid transaminase 1 C12orf24: encoding protein FAM216A C12orf42: encoding protein ...
... serum glutamate pyruvate transaminase - Serum glutamic oxaloacetic transaminase - serum tumor marker test - sesquiterpene ... tyrosine kinase inhibitor - TZT-1027 ubiquinone - UCN-01 - UGT1A1 - ultrasonogram - ultrasonography - ultrasound-guided biopsy- ... aspartate transaminase - aspergillosis - Aspergillus - asthenia - astrocyte - astrocytoma - asymptomatic - atamestane - ataxia ...
Enzymes utilizing such cofactors include the PLP-dependent enzyme aspartate transaminase and the TPP-dependent enzyme pyruvate ... tyrosine, lysine and arginine, as well as serine and threonine. In addition, the peptide backbone, with carbonyl and amide N ...
... tyrosine 2,3-aminomutase EC 5.4.3.7: leucine 2,3-aminomutase EC 5.4.3.8: glutamate-1-semialdehyde 2,1-aminomutase EC 5.4.3.9: ... glutamine-fructose-6-phosphate transaminase (isomerizing) EC 5.3.1.20: ribose isomerase EC 5.3.1.21: corticosteroid side-chain- ...
In addition, PLP is used by aminotransferases (or transaminases) that act upon unusual sugars such as perosamine and desosamine ... generally tyrosine (which may also partake in the acid-base catalysis). Despite the limited requirements for a PLP binding ... liver cysteine desulfhydrase activity disappears and serine and threonine dehydrase and alanine glutamate transaminase ...
Tyrosine Transaminase Grants and funding * HL 18178/HL/NHLBI NIH HHS/United States ... There was a marked induction of tyrosine aminotransferase (TAT) by dexamethasone, which was maintained for up to 72 hr ...
Tyrosine aminotransferase (or tyrosine transaminase) is an enzyme present in the liver and catalyzes the conversion of tyrosine ... Dietrich JB (April 1992). "Tyrosine aminotransferase: a transaminase among others?". Cellular and Molecular Biology. 38 (2): 95 ... L-tyrosine + 2-oxoglutarate ⇌ {\displaystyle \rightleftharpoons } 4-hydroxyphenylpyruvate + L-glutamate In humans, the tyrosine ... and elevated blood tyrosine levels. Keratitis in Tyrosinemia type II patients is caused by the deposition of tyrosine crystals ...
Tyrosine-alpha-ketoglutarate transaminase: induction by epinephrine and adenosine-3,5-cyclic phosphate. Wicks WD. Wicks WD. ... Differences in rates of tyrosine aminotransferase deinduction with cyclic AMP and glucocorticoids. Lewis EJ, Calie P, Wicks WD. ...
5) Tyrosine transaminase activity was significantly diminished by amino-oxyacetate only and showed a late increase after ... of glutamate decarboxylase and of tyrosine transaminase in the brain. (2) The majority of excitatory agents tested (i.e. ...
Liver glucose-6- phosphatase (G-6-Pase), liver alkaline-phosphatase (AP), tyrosine- transaminase (TT), plasma AP, and alanine- ... transaminase (AT) were determined in homogenized liver by undisclosed biochemical methods. Liver AP activity was increased ...
Induction of tyrosine alpha-ketoglutarate transaminase by steroid hormones in a newly established tissue culture cell line. ... Induction of tyrosine alpha-ketoglutarate transaminase by steroid hormones in a newly established tissue culture cell line. ... The interaction of Src and RACK1 is enhanced by activation of protein kinase C and tyrosine phosphorylation of RACK1. J. Biol. ... The interaction of Src and RACK1 is enhanced by activation of protein kinase C and tyrosine phosphorylation of RACK1. J. Biol. ...
Morphine inhibition of the insulin-inducible form of hepatic tyrosine aminotransferase. Sumantra Das, Tapan K. Chatterjee, ... Dive into the research topics of Morphine inhibition of the insulin-inducible form of hepatic tyrosine aminotransferase. ...
g-Aminobutyric acid (GABA) transaminase deficiency. Tyrosine hydroxylase deficiency. Disorders of porphyrin metabolism ( ... tyrosine (a primary marker for tyrosinemia), and immunoreactive trypsinogen (a primary marker for cystic fibrosis) (30). The ...
Tyrosine transaminase family protein. tyrosine aminotransferase 7. -0.65. 0.45. -0.45. 115. AT5G54090. DNA mismatch repair ... are secreted, tyrosine-sulfated, and expressed mainly in. the stem cell area and the innermost layer of central. columella ...
Tyrosine Metabolism Disorders - Etiology, pathophysiology, symptoms, signs, diagnosis & prognosis from the MSD Manuals - ... If expression of a trait requires only one copy of a gene (one allele)... read more disorder is caused by tyrosine transaminase ... There are numerous disorders of phenylalanine and tyrosine metabolism (see the table Phenylalanine and Tyrosine Metabolism ... Tyrosine is an amino acid that is a precursor of several neurotransmitters (eg, dopamine, norepinephrine, epinephrine), ...
REGULATION OF PHOSPHOENOLPYRUVATE CARBOXYKINASE AND TYROSINE TRANSAMINASE IN HEPATOMA CELL CULTURES : III. Comparative Studies ... View Articletitled, REGULATION OF PHOSPHOENOLPYRUVATE CARBOXYKINASE AND TYROSINE TRANSAMINASE IN HEPATOMA CELL CULTURES ,span ...
Tryptophan pyrrolase, tryptophan and tyrosine transaminase changes during allylisopropylacetamide-induced porphyria in the rat ...
Enzymes: choline acetyltransferase; dopamine beta-hydroxylase; GABA transaminase; glutamic acid decarboxylase; glutaminergic; ... phosphodiesterases; tyrosine hydroxylase.. * Intracellular targets: gene expression/transcription markers; markers of ...
... tyrosine transaminase. Urea and albumin secretion was higher in liver organoids compared to hFLPs in 2D culture. These ...
L-tyrosine reversible transport via proton symport (periplasm). TYRTA. Tyrosine transaminase. TYRTRS ...
Glutamic-Oxaloacetic Transaminase 1, Tyrosine-protein kinase Met (c-Met), peroxisome proliferator-activated receptor γ, ...
Tyrosine transaminase, chloroplast. TYRth. Tyrosine permease, chloroplast. Report an error on this page ? ...
... tyrosine transaminase deficiency, systemic lysosomal storage diseases, and several skin diseases X-linked ichthyosis, keratosis ...
"Tyrosine transaminase family protein","protein_coding" "AT2G43100","ATLEUD1","Arabidopsis thaliana","isopropylmalate isomerase ...
Inhibition by aflatonin B-1 of hydrocortisone induction of rat liver tryptophan pyrrolase and tyrosine transaminase. Archives ... Pösö, H.; Pösö, A.R. 1980: Inhibition by aliphatic alcohols of the stimulated activity of ornithine decarboxylase and tyrosine ... Colombo, L.; Carraro, A.; Mauri, M.; Caviezel, F. 1970: Inhibiting effect of tyrosine on the alteration of luteinizing function ... Aragón, M.C.; Giménez, C.; Valdivieso, F. 1982: Inhibition by L-phenylalanine of tyrosine transport by synaptosomal plasma ...
Heilbronn J, Wilson J, Berger BJ: Tyrosine aminotransferase catalyzes the final step of methionine recycling in Klebsiella ... However the bulk of the activity resulted from transaminase YbgE, using either branched chain aminoacids or phenylalanine or ... pneumoniae it is the same enzyme that makes methionine from KMTB and tyrosine from its ketoacid precursor [34]. ... tyrosine as donors could also perform a similar reaction [32]. In K. ...
... spectroscopy starve statistically structure synthesis target targeted transaminase transfer treated treatment triple tyrosine ... increases of glutamate and tyrosine following treatment with 2mM AOA for 24h. Lactate production and glucose consumption in ...
aromatic-amino-acid transaminase TyrB; EC 2.6.1.57 (characterized). 85%. 100%. 679.5. Tyrosine aminotransferase; TyrAT; ... aromatic-amino-acid transaminase TyrB; EC 2.6.1.57 (characterized). 43%. 100%. 331.3. aspartate transaminase (EC 2.6.1.1). 93% ... Branched-chain-amino-acid transaminase (EC 2.6.1.42) (characterized). 100%. 100%. 779.2. kynurenine-oxoglutarate transaminase ( ... 4 candidates for ilvE: isoleucine transaminase. Score. Gene. Description. Similar to. Id.. Cov.. Bits. Other hit. Other id.. ...
... transaminases and are auxotrophic for aspartic acid, isoleucine, leucine, phenylananine, tyrosine, and valine residues. ... Deficient in the aromatic (TyrB), branched-chain (JIvE), and aspartate (AspC) transaminases. ...
TYRB_KLEPN / O85746: Tyrosine aminotransferase; TyrAT; Aromatic-amino-acid transaminase; Aspartate aminotransferase; EC 2.6.1.5 ... oxoglutarate transaminase 4; Kynurenine--oxoglutarate transaminase IV; Transaminase A; EC 2.6.1.1; EC 2.6.1.7 from Danio rerio ... oxoglutarate transaminase 4; Kynurenine--oxoglutarate transaminase IV; Transaminase A; EC 2.6.1.1; EC 2.6.1.7 from Danio rerio ... oxoglutarate transaminase 4; Kynurenine--oxoglutarate transaminase IV; Transaminase A; EC 2.6.1.1; EC 2.6.1.7 from Gallus ...
2.6 GABA transaminase. *2.7 Nucleotidyltransferase *Integrase. *Reverse transcriptase. *Protein kinase *Tyrosine kinase *Janus ...
Tyrosine Transaminase has restriction * closed Date in CU Experts * October 1, 2013 11:33 AM ...
IGF012/81 (skin, fibroblast, tyrosine transaminase deficiency) - GEIMM. IGF012/82 (skin, fibroblast) - GEIMM. IGF012/83 (skin, ... IGF017/82 (skin, fibroblast, tyrosine transaminase deficiency) - GEIMM. IGF017/83 (skin, fibroblast) - GEIMM. IGF017/84 (skin, ... IGF130/82 (skin, fibroblast, tyrosine transaminase deficiency) - GEIMM. IGF130/83 (skin, fibroblast, Lesch-Nyhan syndrome) - ... IGF013/81 (skin, fibroblast, tyrosine transaminase deficiency) - GEIMM. IGF013/82 (skin, fibroblast, mucopolysaccharidosis type ...
4-dihydroxyphenylalanine transaminase). In addition to L-dopa, the enzyme can also use L-tyrosine, L-phenylalanine, L- ... tyrosine or tryptophan. The enzyme from Sinorhizobium meliloti requires a divalent cation for activity and can hydrolyse N- ...
Tyrosine is generally classified as a hydrophobic amino acid, it is more hydrophilic than phenylalanine. ... para-hydroxyphenylalanine) begins with an α-ketoglutarate dependent transamination through the tyrosine transaminase to para- ... Tyrosine Explained. -Tyrosine or tyrosine (symbol Tyr or Y)[1] or 4-hydroxyphenylalanine is one of the 20 standard amino acids ... It transforms L-tyrosine into p-coumaric acid.Tyrosine is also the precursor to the pigment melanin. Tyrosine (or its precursor ...

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