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Isolation and properties of a new glutamine transaminase from rat kidney.

作者信息

Cooper A J, Meister A

出版信息

J Biol Chem. 1974 Apr 25;249(8):2554-61.

PMID:4822504
Abstract
摘要

相似文献

1
Isolation and properties of a new glutamine transaminase from rat kidney.
J Biol Chem. 1974 Apr 25;249(8):2554-61.
2
High activities of glutamine transaminase K (dichlorovinylcysteine beta-lyase) and omega-amidase in the choroid plexus of rat brain.大鼠脑脉络丛中谷氨酰胺转氨酶K（二氯乙烯基半胱氨酸β-裂解酶）和ω-酰胺酶的高活性。
J Neurochem. 1993 Nov;61(5):1731-41. doi: 10.1111/j.1471-4159.1993.tb09810.x.
3
Glutamine transaminase K from rat kidney.
Methods Enzymol. 1985;113:344-9. doi: 10.1016/s0076-6879(85)13047-8.
4
The source of aromatic ketoacids in tyrosinaemia and phenylketonuria.酪氨酸血症和苯丙酮尿症中芳香族酮酸的来源。
Clin Chim Acta. 1972 Jun;39(1):243-6. doi: 10.1016/0009-8981(72)90323-3.
5
Regional and subcellular distribution of aminotransferases in rat brain.大鼠脑中氨基转移酶的区域和亚细胞分布。
J Neurochem. 1972 Apr;19(4):949-57. doi: 10.1111/j.1471-4159.1972.tb01416.x.
6
Purification of soluble and mitochondrial glutamine transaminase K from rat kidney. Use of a sensitive assay involving transamination between L-phenylalanine and alpha-keto-gamma-methiolbutyrate.从大鼠肾脏中纯化可溶性和线粒体谷氨酰胺转氨酶K。使用一种涉及L-苯丙氨酸与α-酮-γ-甲硫基丁酸之间转氨作用的灵敏检测方法。
Anal Biochem. 1978 Sep;89(2):451-60. doi: 10.1016/0003-2697(78)90374-3.
7
Evidence of phenylalanine transaminase activity in the isoenzymes of aspartate transaminase.天冬氨酸转氨酶同工酶中苯丙氨酸转氨酶活性的证据。
J Biol Chem. 1972 Apr 25;247(8):2486-92.
8
Branched chain aminotransferase isoenzymes. Purification and characterization of the rat brain isoenzyme.支链氨基转移酶同工酶。大鼠脑同工酶的纯化与特性鉴定。
J Biol Chem. 1993 Feb 15;268(5):3092-8.
9
[Metabolism of phenylalanine and tyrosine and regulation by thyroid hormones in albino rat brain].[白化大鼠脑中苯丙氨酸和酪氨酸的代谢及甲状腺激素的调节]
Biokhimiia. 1966 Mar-Apr;31(2):265-9.
10
Purification, characterization and identification of aromatic 2-oxo acid reductase.芳香族2-氧代酸还原酶的纯化、表征与鉴定。
Life Sci. 1977 Feb 15;20(4):609-16. doi: 10.1016/0024-3205(77)90463-5.

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Front Oncol. 2023 Mar 7;13:1143798. doi: 10.3389/fonc.2023.1143798. eCollection 2023.
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α-Ketoglutaramate-A key metabolite contributing to glutamine addiction in cancer cells.
α-酮戊二酸——癌细胞中导致谷氨酰胺成瘾的关键代谢物。
Front Med (Lausanne). 2022 Nov 4;13:1035335. doi: 10.3389/fmed.2022.1035335. eCollection 2022.
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Comprehensive Metabolic Profiling of MYC-Amplified Medulloblastoma Tumors Reveals Key Dependencies on Amino Acid, Tricarboxylic Acid and Hexosamine Pathways.MYC 扩增的髓母细胞瘤肿瘤的综合代谢谱分析揭示了对氨基酸、三羧酸和己糖胺途径的关键依赖性。
Cancers (Basel). 2022 Mar 3;14(5):1311. doi: 10.3390/cancers14051311.
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High Levels of Glutaminase II Pathway Enzymes in Normal and Cancerous Prostate Suggest a Role in 'Glutamine Addiction'.高水平的谷氨酰胺酶 II 通路酶在正常和癌变前列腺中提示其在“谷氨酰胺成瘾”中的作用。
Biomolecules. 2019 Dec 18;10(1):2. doi: 10.3390/biom10010002.
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Kynurenine aminotransferase 3/glutamine transaminase L/cysteine conjugate beta-lyase 2 is a major glutamine transaminase in the mouse kidney.犬尿氨酸转氨酶3/谷氨酰胺转氨酶L/半胱氨酸共轭β-裂解酶2是小鼠肾脏中的一种主要谷氨酰胺转氨酶。
Biochem Biophys Rep. 2016 Sep 21;8:234-241. doi: 10.1016/j.bbrep.2016.09.008. eCollection 2016 Dec.
7
Fluorination at the 4 position alters the substrate behavior of L-glutamine and L-glutamate: Implications for positron emission tomography of neoplasias.4位的氟化作用改变了L-谷氨酰胺和L-谷氨酸的底物行为：对肿瘤正电子发射断层扫描的意义。
J Fluor Chem. 2016 Dec;192(A):58-67. doi: 10.1016/j.jfluchem.2016.10.008. Epub 2016 Oct 20.
8
Kynurenine aminotransferase III and glutamine transaminase L are identical enzymes that have cysteine S-conjugate β-lyase activity and can transaminate L-selenomethionine.犬尿氨酸氨基转移酶 III 和谷氨酰胺转氨酶 L 是同一种酶，具有半胱氨酸 S- 共轭 β- 裂合酶活性，并且可以转氨基 L- 硒代蛋氨酸。
J Biol Chem. 2014 Nov 7;289(45):30950-61. doi: 10.1074/jbc.M114.591461. Epub 2014 Sep 17.
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α-Ketoglutaramate: an overlooked metabolite of glutamine and a biomarker for hepatic encephalopathy and inborn errors of the urea cycle.α-酮戊二酸：一种被忽视的谷氨酰胺代谢产物以及肝性脑病和尿素循环先天性代谢缺陷的生物标志物。
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Increase in cystathionine content in rat liver mitochondria after D,L-propargylglycine administration.D,L-炔丙基甘氨酸给药后大鼠肝线粒体胱硫醚含量增加。
Amino Acids. 1995 Jun;9(2):111-22. doi: 10.1007/BF00805832.