8DEB

Bacteroides fragilis carboxyspermidine dehydrogenase

8DEB の概要

• エントリーDOI: 10.2210/pdb8deb/pdb
• 分子名称: Carboxyspermidine dehydrogenase, NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE (3 entities in total)
• 機能のキーワード: spermidine, norspermidine, dehydrogenase, polyamine, carboxyspermidine, carboxynorspermidine, biosynthetic protein
• 由来する生物種: Bacteroides fragilis
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 91734.25

構造登録者

McFarlane, J.S.,Bouchey, S.,Dodd, J. (登録日: 2022-06-20, 公開日: 2023-08-02, 最終更新日: 2026-03-04)

主引用文献

Lee, D.F.,Atencio, N.,Bouchey, S.,Shoemaker, M.R.,Dodd, J.S.,Satre, M.,Miller, K.A.,McFarlane, J.S.
Kinetic and structural characterization of carboxyspermidine dehydrogenase of polyamine biosynthesis.
J.Biol.Chem., 299:105033-105033, 2023

PubMed Abstract: Polyamines are positively charged alkylamines ubiquitous among eukaryotes, prokaryotes, and archaea. Humans obtain polyamines through dietary intake, metabolic production, or uptake of polyamines made by gut microbes. The polyamine biosynthetic pathway used by most gut microbes differs from that used by human cells. This alternative pathway employs carboxyspermidine dehydrogenase (CASDH), an enzyme with limited characterization. Here, we solved a 1.94 Å X-ray crystal structure of Bacteroides fragilis CASDH by molecular replacement. BfCASDH is composed of three domains with a fold similar to saccharopine dehydrogenase but with a distinct active site arrangement. Using steady-state methods, we determined k and k/K for BfCASDH and Clostridium leptum CASDH using putrescine, diaminopropane, aspartate semi-aldehyde, NADH, and NADPH as substrates. These data revealed evidence of cooperativity in BfCASDH. Putrescine is the likely polyamine substrate and NADPH is the coenzyme used to complete the reaction, forming carboxyspermidine as a product. These data provide the first kinetic characterization of CASDH-a key enzyme in the production of microbial polyamines.

PubMed: 37437886
DOI: 10.1016/j.jbc.2023.105033

実験手法

X-RAY DIFFRACTION (1.94 Å)