Literature summary for 2.4.1.267 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 .

Search for more literature for 2.4.1.267

Crystallization (Commentary)

Crystallization (Comment)	Organism
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

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

General Stability

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

Inhibitors

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

Metals/Ions

Metals/Ions	Comment	Organism	Structure
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

Organism	UniProt	Comment	Textmining
Saccharomyces cerevisiae	Q12001	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
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	-	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	-	?
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

Synonyms	Comment	Organism
ALG6	-	Saccharomyces cerevisiae

General Information

General Information	Comment	Organism
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

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)