TerC Proteins Function During Protein Secretion to Metalate Exoenzymes

bioRxiv (Cold Spring Harbor Laboratory), Год журнала: 2023, Номер unknown

Опубликована: Апрель 10, 2023

Cytosolic metalloenzymes acquire metals from buffered intracellular pools. How exported are appropriately metalated is less clear. We provide evidence that TerC family proteins function in metalation of enzymes during export through the general secretion (Sec-dependent) pathway. Bacillus subtilis strains lacking MeeF(YceF) and MeeY(YkoY) have a reduced capacity for protein greatly level manganese (Mn) secreted proteome. MeeF MeeY copurify with secretory pathway, their absence FtsH membrane protease essential viability. also required efficient Mn 2+ -dependent lipoteichoic acid synthase (LtaS), membrane-localized enzyme an extracytoplasmic active site. Thus, MeeY, representative widely conserved transporters, co-translocational extracellular enzymes.

Язык: Английский

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TerC Proteins Function During Protein Secretion to Metalate Exoenzymes

Research Square (Research Square), Год журнала: 2023, Номер unknown

Опубликована: Май 17, 2023

Cytosolic metalloenzymes acquire metals from buffered intracellular pools. How exported are appropriately metalated is less clear. We provide evidence that TerC family proteins function in metalation of enzymes during export through the general secretion (Sec-dependent) pathway. Bacillus subtilis strains lacking MeeF(YceF) and MeeY(YkoY) have a reduced capacity for protein greatly level manganese (Mn) secreted proteome. MeeF MeeY copurify with secretory pathway, their absence FtsH membrane protease essential viability. also required efficient Mn2+-dependent lipoteichoic acid synthase (LtaS), membrane-localized enzyme an extracytoplasmic active site. Thus, MeeY, representative widely conserved transporters, co-translocational extracellular enzymes.

Язык: Английский

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Identification of an Additional Metal-Binding Site in Human Dipeptidyl Peptidase III

International Journal of Molecular Sciences, Год журнала: 2023, Номер 24(16), С. 12747 - 12747

Опубликована: Авг. 13, 2023

Dipeptidyl peptidase III (DPP III, EC 3.4.14.4) is a monozinc metalloexopeptidase that hydrolyzes dipeptides from the N-terminus of peptides consisting three or more amino acids. Recently, DPP has attracted great interest scientists, and numerous studies have been conducted showing it involved in regulation various physiological processes. Since only metalloenzyme among dipeptidyl peptidases, we considered important to study process binding exchange physiologically relevant metal dications III. Using fluorimetry, measured Kd values for Zn2+, Cu2+, Co2+ catalytic site, using isothermal titration calorimetry (ITC), these metals an additional site. The structure metal’s site known previous studies, this work, affinities were calculated Co2+, Mn2+ QM approach. structures sites Zn2+ Cu2+ also identified, MD simulations showed two ions bound inhibitory exchanged less frequently than sites.

Язык: Английский

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Structural and biochemical characterisation of the N‐carbamoyl‐β‐alanine amidohydrolase from Rhizobium radiobacterMDC 8606

FEBS Journal, Год журнала: 2023, Номер 290(23), С. 5566 - 5580

Опубликована: Авг. 27, 2023

N-carbamoyl-β-alanine amidohydrolase (CβAA) constitutes one of the most important groups industrially relevant enzymes used in production optically pure amino acids and derivatives. In this study, a CβAA-encoding gene from Rhizobium radiobacter strain MDC 8606 was cloned overexpressed Escherichia coli. The purified recombinant enzyme (RrCβAA) showed specific activity 14 U·mg

Язык: Английский

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