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Literature summary extracted from

  • Bloch, J.S.; Pesciullesi, G.; Boilevin, J.; Nosol, K.; Irobalieva, R.N.; Darbre, T.; Aebi, M.; Kossiakoff, A.A.; Reymond, J.L.; Locher, K.P.
    Structure and mechanism of the ER-based glucosyltransferase ALG6 (2020), Nature, 579, 443-447 .
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.4.1.267 structure of nanodisc-reconstituted apo-ALG6 at 3 A resolution. ALG6 has 14 transmembrane helices and two long loops (EL1 and EL4) that form helices in the ER lumen. The first external loop contains the catalytically essential residue Asp69 Saccharomyces cerevisiae

Protein Variants

EC Number Protein Variants Comment Organism
2.4.1.267 D307A activity is unaffected by the mutation Saccharomyces cerevisiae
2.4.1.267 D69A loss of activity Saccharomyces cerevisiae
2.4.1.267 D69N strong reduction of activity Saccharomyces cerevisiae
2.4.1.267 D99A loss of activity Saccharomyces cerevisiae
2.4.1.267 D99N activity is unaffected by the mutation Saccharomyces cerevisiae
2.4.1.267 E306A activity is unaffected by the mutation Saccharomyces cerevisiae
2.4.1.267 E379A activity is unaffected by the mutation Saccharomyces cerevisiae
2.4.1.267 H378A strong reduction of activity Saccharomyces cerevisiae
2.4.1.267 H378D strong reduction of activity Saccharomyces cerevisiae
2.4.1.267 H378E strong reduction of activity Saccharomyces cerevisiae

General Stability

EC Number General Stability Organism
2.4.1.267 ALG6 is active in different detergents as well as reconstituted in lipid nanodiscs Saccharomyces cerevisiae

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.4.1.267 additional information not inhibitory: EDTA Saccharomyces cerevisiae

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.4.1.267 additional information no evidence for metal ions in the crystal structure, nor presence of a DXD motif. Reaction is metal-ion independent Saccharomyces cerevisiae

Organism

EC Number Organism UniProt Comment Textmining
2.4.1.267 Saccharomyces cerevisiae Q12001
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-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.4.1.267 dolichyl beta-D-glucosyl phosphate + alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphospho-Dol25
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 Saccharomyces cerevisiae alpha-D-Glc-(1->3)-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphospho-Dol25 + dolichyl phosphate
-
 ?
2.4.1.267 dolichyl beta-D-glucosyl phosphate + alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphosphodolichol
-
 Saccharomyces cerevisiae alpha-D-Glc-(1->3)-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphosphodolichol + dolichyl phosphate
-
 ?

Synonyms

EC Number Synonyms Comment Organism
2.4.1.267 ALG6
-
 Saccharomyces cerevisiae

General Information

EC Number General Information Comment Organism
2.4.1.267 physiological function three-state mechanism, where Dol-P-Glc binds before the Man9-containing acceptor substrate, because the glucose moiety is at the bottom of the active site cavity. Donor and acceptor substrates bind sequentially and Asp69 acts as a general base that abstracts the proton of the 3-hydroxyl group of the terminal A-branch mannose of the acceptor substrate to activate it for a nucleophilic attack Saccharomyces cerevisiae