5MR0

Thermophilic archaeal branched-chain amino acid transaminases from Geoglobus acetivorans and Archaeoglobus fulgidus: biochemical and structural characterisation

5MR0 の概要

• エントリーDOI: 10.2210/pdb5mr0/pdb
• 分子名称: Putative branched-chain-amino-acid aminotransferase, 3-[O-PHOSPHONOPYRIDOXYL]--AMINO-BENZOIC ACID, CHLORIDE ION, ... (8 entities in total)
• 機能のキーワード: thermophilic archaea, branch-chain transaminases, substrate specificity, transferase
• 由来する生物種: Archaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126); 詳細
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 198150.25

構造登録者

Isupov, M.N.,Littlechild, J.A.,James, P.,Sayer, C.,Sutter, J.M.,Schmidt, M.,Schoenheit, P. (登録日: 2016-12-21, 公開日: 2018-01-17, 最終更新日: 2024-01-17)

主引用文献

Isupov, M.N.,Boyko, K.M.,Sutter, J.M.,James, P.,Sayer, C.,Schmidt, M.,Schonheit, P.,Nikolaeva, A.Y.,Stekhanova, T.N.,Mardanov, A.V.,Ravin, N.V.,Bezsudnova, E.Y.,Popov, V.O.,Littlechild, J.A.
Thermostable Branched-Chain Amino Acid Transaminases From the ArchaeaGeoglobus acetivoransandArchaeoglobus fulgidus: Biochemical and Structural Characterization.
Front Bioeng Biotechnol, 7:7-7, 2019

PubMed Abstract: Two new thermophilic branched chain amino acid transaminases have been identified within the genomes of different hyper-thermophilic archaea, , and . These enzymes belong to the class IV of transaminases as defined by their structural fold. The enzymes have been cloned and over-expressed in and the recombinant enzymes have been characterized both biochemically and structurally. Both enzymes showed high thermostability with optimal temperature for activity at 80 and 85°C, respectively. They retain good activity after exposure to 50% of the organic solvents, ethanol, methanol, DMSO and acetonitrile. The enzymes show a low activity to ()-methylbenzylamine but no activity to ()-methylbenzylamine. Both enzymes have been crystallized and their structures solved in the internal aldimine form, to 1.9 Å resolution for the enzyme and 2.0 Å for the enzyme. Also the enzyme structure has been determined in complex with the amino acceptor α-ketoglutarate and the enzyme in complex with the inhibitor gabaculine. These two complexes have helped to determine the conformation of the enzymes during enzymatic turnover and have increased understanding of their substrate specificity. A comparison has been made with another () selective class IV transaminase from the fungus which was previously studied in complex with gabaculine. The subtle structural differences between these enzymes has provided insight regarding their different substrate specificities.

PubMed: 30733943
DOI: 10.3389/fbioe.2019.00007

実験手法

X-RAY DIFFRACTION (1.98 Å)