WordNet

undergo transfer from one compound to another; "amino groups can transaminate"
change (an amino group) by transferring it from one compound to another
the process of transfering an amino group from one compound to another
the process of transposing an amino group within a chemical compound

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1. 肝機能検査値異常が認められた患者に対するアプローチ approach to the patient with abnormal liver function tests
2. 肝疾患の有無と血漿中のアスパラギン酸アミノトランスフェラーゼおよびアラニン・
アミノトランスフェラーゼ濃度のパターン patterns of plasma aspartate and alanine aminotransferase levels with and without liver disease
3. 小児および思春期の患者におけるアセトアミノフェン（パラセタモール）中毒の
臨床症状および診断 clinical manifestations and diagnosis of acetaminophen paracetamol poisoning in children and adolescents
4. 肝細胞障害を検出する肝機能検査 liver function tests that detect injury to hepatocytes
5. 血清アミノトランスフェラーゼ値が正常な慢性C型肝炎ウイルス感染患者へのアプローチ approach to patients with chronic hepatitis c virus infection and normal serum aminotransferases

English Journal

Isolation, purification, and characterization of phenylpyruvate transaminating enzymes of Erwinia carotovora.

Paloyan AM1, Hambardzumyan AA, Halebyan GP.Author information 1SPC Armbiotechnology, National Academy of Sciences of Republic of Armenia, Yerevan, Republic of Armenia. arm_biotech@yahoo.comAbstractEnzymes of Erwinia carotovora that transaminate phenylpyruvate were isolated, purified, and characterized. Two aromatic aminotransferases (PAT1 and PAT2) and an aspartic aminotransferase (PAT3) were found. According to gel filtration, these enzymes have molecular weights of 76, 75, and 78 kDa. The enzymes consist of two identical subunits of molecular weights of 31.4, 31, and 36.5 kDa, respectively. The isoelectric points of PAT1, PAT2, and PAT3 were determined as 3.6, 3.9, and 4.7, respectively. The enzyme preparations considerably differ in substrate specificity. All three of the enzymes productively interacted with the following amino acids: L-aspartic acid, L-leucine (except PAT3), L-isoleucine (except PAT3), L-serine, L-methionine, L-cysteine, L-phenylalanine, L-tyrosine, and L-tryptophane. The aromatic aminotransferases display higher specificity to the aromatic amino acids and the leucine-isoleucine pair, whereas the aspartic aminotransferase displays higher specificity to L-aspartic acid and relatively low specificity to the aromatic amino acids. The aspartic aminotransferase does not use L-leucine or L-isoleucine as a substrate. PAT1, PAT2, and PAT3 show the highest activity at pH 8.9 and at 48, 53, and 58°C, respectively.
Biochemistry. Biokhimii͡a.Biochemistry (Mosc).2012 Jan;77(1):98-104. doi: 10.1134/S0006297912010129.
Enzymes of Erwinia carotovora that transaminate phenylpyruvate were isolated, purified, and characterized. Two aromatic aminotransferases (PAT1 and PAT2) and an aspartic aminotransferase (PAT3) were found. According to gel filtration, these enzymes have molecular weights of 76, 75, and 78 kDa. The e
PMID 22339639

Dihydrophenylalanine: a prephenate-derived Photorhabdus luminescens antibiotic and intermediate in dihydrostilbene biosynthesis.

Crawford JM1, Mahlstedt SA, Malcolmson SJ, Clardy J, Walsh CT.Author information 1Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA 02115, USA.Abstract2,5-Dihydrophenylalanine (H(2)Phe) is a multipotent nonproteinogenic amino acid produced by various Actinobacteria and Gammaproteobacteria. Although the metabolite was discovered over 40 years ago, details of its biosynthesis have remained largely unknown. We show here that L-H(2)Phe is a secreted metabolite in Photorhabdus luminescens cultures and a precursor of a recently described 2,5-dihydrostilbene. Bioinformatic analysis suggested a candidate gene cluster for the processing of prephenate to H(2)Phe, and gene knockouts validated that three adjacent genes plu3042-3044 were required for H(2)Phe production. Biochemical experiments validated Plu3043 as a nonaromatizing prephenate decarboxylase generating an endocyclic dihydro-hydroxyphenylpyruvate. Plu3042 acted next to transaminate the Plu3043 product, precluding spontaneous exocyclic double-bond isomerization and yielding 2,5-dihydrotyrosine. The enzymatic products most plausibly on path to H(2)Phe illustrate the versatile metabolic rerouting of prephenate from aromatic amino acid synthesis to antibiotic synthesis.
Chemistry & biology.Chem Biol.2011 Sep 23;18(9):1102-12. doi: 10.1016/j.chembiol.2011.07.009.
2,5-Dihydrophenylalanine (H(2)Phe) is a multipotent nonproteinogenic amino acid produced by various Actinobacteria and Gammaproteobacteria. Although the metabolite was discovered over 40 years ago, details of its biosynthesis have remained largely unknown. We show here that L-H(2)Phe is a secreted m
PMID 21944749

The oxidoreductases LivQ and NeoQ are responsible for the different 6'-modifications in the aminoglycosides lividomycin and neomycin.

Clausnitzer D1, Piepersberg W, Wehmeier UF.Author information 1BU Wuppertal, FB-C, Chemical Microbiology AG, Piepersberg, Wuppertal, Germany.AbstractAIMS: The 2-deoxystreptamine-containing aminoglycoside antibiotics (AGAs) constitute the largest subgroup of the aminoglycosides. Neomycin (NEO) and lividomycin (LIV) are both representatives of the pseudo-tetrasaccharide group among the NEO-type AGAs. While NEO contains a 6'-NH(2) group, the 6'-position remains unmodified in LIV. The aim of the study was to characterize the substrate specificities of the enzymes involved in the C-6'- and C-6‴-modification in order to explain the different amination patterns.
Journal of applied microbiology.J Appl Microbiol.2011 Sep;111(3):642-51. doi: 10.1111/j.1365-2672.2011.05082.x. Epub 2011 Jul 12.
AIMS: The 2-deoxystreptamine-containing aminoglycoside antibiotics (AGAs) constitute the largest subgroup of the aminoglycosides. Neomycin (NEO) and lividomycin (LIV) are both representatives of the pseudo-tetrasaccharide group among the NEO-type AGAs. While NEO contains a 6'-NH(2) group, the 6'-pos
PMID 21689223

High rates and substrate selectivities in water by polyvinylimidazoles as transaminase enzyme mimics with hydrophobically bound pyridoxamine derivatives as coenzyme mimics.

Skouta R1, Wei S, Breslow R.Author information 1Department of Chemistry, Columbia University, New York, New York 10027, USA.AbstractFree-radical polymers of 4-vinylimidazole and copolymers with 1-dodecyl-4-vinylimidazole were used as enzyme mimics to transaminate pyruvic acid to alanine, phenylpyruvic acid to phenylalanine, and indole-3-pyruvic acid to tryptophan in water at pH 7.5 and 20 degrees C using pyridoxamines carrying hydrophobic side chains as coenzyme mimics. The best enzyme mimic accelerated the transamination of indole-3-pyruvic acid by a factor of 4 million relative to the rate without the polymer, a higher rate ratio than we had previously achieved with a polyaziridine-based enzyme mimic. The properties of various polyvinylimidazoles were compared, including those prepared with the RAFT modification of the polymerization process.
Journal of the American Chemical Society.J Am Chem Soc.2009 Nov 4;131(43):15604-5. doi: 10.1021/ja9072589.
Free-radical polymers of 4-vinylimidazole and copolymers with 1-dodecyl-4-vinylimidazole were used as enzyme mimics to transaminate pyruvic acid to alanine, phenylpyruvic acid to phenylalanine, and indole-3-pyruvic acid to tryptophan in water at pH 7.5 and 20 degrees C using pyridoxamines carrying h
PMID 19824661

Japanese Journal

脳のアミノ酸代謝に関する研究第II編脳トランスアミナーゼに関する研究

国土忠男
岡山医学会雑誌 71(9-1), 5651-5657, 1959-08-30
… The activities of aspartic-glutamic transaminase and γ-aminobutyric-glutamic transaminate in rabbit brain and human cerbral cortex were determined. …
NAID 120002689843