Source:
Generated By: https://synbiohub.org/public/igem/igem2sbol/1
Created by: Larissa Kr??ger
Date created: 2016-10-12 11:00:00
Date modified: 2016-10-13 04:56:34
TorA-GlmS
| Types | DnaRegion |
| Roles | engineered_region Composite |
| Sequences | BBa_K1978001_sequence (Version 1) |
Description
The TorA-GlmS Biobrick consists of a TorA signal linked to GlmS, which is a vitamin B12 binding protein. The TorA signal sequence allows export of fully-folded proteins through the inner membrane via the TAT(Twin-Arginin)export system. This enables export of vitamin B12 out of the cell.The TorA sequence codes for a peptide that harbours a twin-arginine motif. This is vital for the recognition by the Tat system. Moreover, an AxA motif is present, which leads to cleavage by the leader peptidase I (Palmer & Berks 2012).
MNNNDLFQASRRRFLAQLGGLTVAGMLGPSLLTPRRATA
GlmS is the B12-binding subunit of glutamate mutase (Glm) from Clostridium cochlearium. The mechanism by which the enzyme uses adenosylcobalamin is highly similar to methylmalonyl coenzyme A mutase. Glm catalyzes the reversible rearrangement of (2S)-glutamate to (2S,3S)-3-methylaspartate (Leutbecher et al., 1992). The assembly of the active enzyme, an α2β2 tetramer, is mediated by coenzyme B12. While GlmS as the smaller subunit (14.8 kDa) binds B12, the larger subunit GlmE harbors the substrate binding site (Zelder et al., 1994).