Sandhu S S, Chase T
Can J Microbiol. 1986 Sep;32(9):743-50. doi: 10.1139/m86-135.
Cleavage of choline to trimethylamine and acetaldehyde by extracts of Proteus mirabilis requires both particulate and soluble protein fractions, K+, and a bound divalent metal cation. The reaction shows a long lag period, abolished only by preincubation of the particulate fraction in the complete reaction system. The two-carbon fragment produced is acetaldehyde; choline cleavage appears to be tightly coupled to dismutation of the acetaldehyde to ethanol and acetate, as indicated by stimulation by NAD+, ADP, and Fe2+ and inhibition by reagents reacting with acetaldehyde. The system is thus similar to that previously described in anaerobes (Desulfovibrio, Clostridium). Attempts to demonstrate a cobamide coenzyme requirement (as in the similar ethanolamine ammonia-lyase reaction) were unsuccessful; the reaction was carried out by fractions devoid of vitamin B12 activity (not supporting growth of Lactobacillus leichmannii) and insensitive to light.
奇异变形杆菌提取物将胆碱裂解为三甲胺和乙醛的过程需要颗粒性和可溶性蛋白质组分、K⁺以及一种结合的二价金属阳离子。该反应呈现出较长的延迟期，只有在完整反应体系中对颗粒性组分进行预孵育才能消除。产生的二碳片段是乙醛；胆碱裂解似乎与乙醛歧化为乙醇和乙酸紧密偶联，这由NAD⁺、ADP和Fe²⁺的刺激以及与乙醛反应的试剂的抑制所表明。因此该体系与先前在厌氧菌（脱硫弧菌、梭菌）中描述的体系相似。试图证明需要钴胺素辅酶（如在类似的乙醇胺氨裂解酶反应中）未成功；该反应由缺乏维生素B₁₂活性（不支持赖氏乳杆菌生长）且对光不敏感的组分进行。
