Members of the Rid protein family have broad imine deaminase activity and can accelerate the Pseudomonas aeruginosa D-arginine dehydrogenase (DauA) reaction in vitro.

Members of the Rid protein family have broad imine deaminase activity and can accelerate the Pseudomonas aeruginosa D-arginine dehydrogenase (DauA) reaction in vitro.
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DOI:
10.1371/journal.pone.0185544
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发表时间:
2017
期刊:
影响因子:
3.7
通讯作者:
Downs DM
Downs DM
中科院分区:
综合性期刊3区
文献类型:
--
作者:
Hodge-Hanson KM;Downs DM

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Rid(YjgF/YER 057 c/UK 114)蛋白家族是一组小的、序列多样的蛋白质,由八个亚家族组成。原型RidA亚家族存在于所有结构域中,而Rid 1 -7亚家族仅存在于原核生物中。细菌基因组通常编码Rid超家族的多个成员。该蛋白质家族的最佳表征成员,来自肠道沙门氏菌的RidA,是一种脱氨酶,其淬灭由吡哆醛5 '-磷酸依赖性酶产生的反应性代谢物2-氨基丙烯酸酯,并最终使某些酶免受损害。2-氨基丙烯酸酯的积累会破坏酶并导致细菌、植物和酵母的生长缺陷。虽然所有的亚家族成员已被注释为亚胺脱氨酶的基础上的RidA表征,实验证据支持这种注释存在于一个单一的蛋白质以外的RidA亚家族。在这里,我们报告说,六种蛋白质,跨越Rid亚家族1-3,脱氨各种亚胺/烯胺底物具有不同的比活性。由铜绿假单胞菌D-精氨酸脱氢酶DauA原位产生的来自Rid 2和Rid 3亚家族的蛋白质,而不是来自RidA和Rid 1亚家族的脱氨基亚氨基精氨酸。这些数据在生物化学上区分了这些亚家族,并显示Rid蛋白对假单胞菌和其他细菌中生理相关的代谢物具有活性。
The Rid (YjgF/YER057c/UK114) protein family is a group of small, sequence diverse proteins that consists of eight subfamilies. The archetypal RidA subfamily is found in all domains, while the Rid1-7 subfamilies are present only in prokaryotes. Bacterial genomes often encode multiple members of the Rid superfamily. The best characterized member of this protein family, RidA from Salmonella enterica, is a deaminase that quenches the reactive metabolite 2-aminoacrylate generated by pyridoxal 5’-phosphate-dependent enzymes and ultimately spares certain enzymes from damage. The accumulation of 2-aminoacrylate can damage enzymes and lead to growth defects in bacteria, plants, and yeast. While all subfamily members have been annotated as imine deaminases based on the RidA characterization, experimental evidence to support this annotation exists for a single protein outside the RidA subfamily. Here we report that six proteins, spanning Rid subfamilies 1–3, deaminate a variety of imine/enamine substrates with differing specific activities. Proteins from the Rid2 and Rid3 subfamilies, but not from the RidA and Rid1 subfamilies deaminated iminoarginine, generated in situ by the Pseudomonas aeruginosa D-arginine dehydrogenase DauA. These data biochemically distinguished the subfamilies and showed Rid proteins have activity on a metabolite that is physiologically relevant in Pseudomonas and other bacteria.
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发表时间: 2002-08-01
期刊: PROTEINS-STRUCTURE FUNCTION AND GENETICS
影响因子: --
作者:
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