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Identification and characterization of two new types of bacterial L-serine dehydratases and assessment of the function of the ACT domain.

Abstract：

:Two new types of bacterial Fe-S L-serine dehydratases have been identified. These join two previously recognized enzyme types, for a total of four, that are distinguished on the basis of domain arrangement and amino acid sequence. A Type 3 enzyme from Amphibacillus xylanus (axLSD) and a Type 4 enzyme from Heliscomenobacter hydrossis (hhLSD) were cloned, expressed, purified, and characterized. Like the Type 1 enzyme from Bacillus subtilis (bsLSD), axLSD required a monovalent cation, preferably potassium, for activity. However, the hhLSD was without activity even after reconstitution of the iron-sulfur center by a process that successfully restored activity to oxygen-inactivated axLSD. This and other characteristics suggest that this Type 4 protein may be a pseudoenzyme. The oxygen sensitivity of axLSD was greater than other L-serine dehydratases so far studied and suggested that there may be significant conformational differences among the four types resulting in widely different solvent accessibility of the Fe-S clusters in these enzymes. The role of the ACT domain in these enzymes was explored by deleting it from bsLSD. Although there was an effect on the kinetic parameters, this domain was not responsible for the cation requirement nor did its removal have a significant effect on oxygen sensitivity.

journal_name

Arch Biochem Biophys

journal_title

Archives of biochemistry and biophysics

authors

Xu XL,Grant GA

doi

10.1016/j.abb.2013.10.009

subject

Has Abstract

pub_date

2013-12-01 00:00:00

pages

62-9

issue

1-2

eissn

0003-9861

issn

1096-0384

pii

S0003-9861(13)00321-4

journal_volume

540

pub_type

杂志文章

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