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Literature summary for 2.4.1.342 extracted from

  • Syson, K.; Stevenson, C.; Lawson, D.; Bornemann, S.
    Structure of the Mycobacterium smegmatis alpha-maltose-1-phosphate synthase GlgM (2020), Acta Crystallogr. Sect. F, 76, 175-181.
    View publication on PubMed
Search for more literature for 2.4.1.342

Crystallization (Commentary)

Crystallization (Comment) Organism
structure at 1.9 A resolution. GlgM shares a GT-B fold with bacterial glycogen synthases Mycolicibacterium smegmatis

Inhibitors

Inhibitors Comment Organism Structure
D-glucose 1-phosphate substrate inhibition above 4 mM Mycolicibacterium smegmatis

Organism

Organism UniProt Comment Textmining
Mycolicibacterium smegmatis A0R2E2
-
-
Mycolicibacterium smegmatis ATCC 700084 A0R2E2
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information enzyme follows a ternary complex mechanism, whereby ADP-glucose binds to the enzyme before D-glucose 1-phosphate. GlgM shows no detecable glycogen synthase activity Mycolicibacterium smegmatis ?
-
 ?
additional information enzyme follows a ternary complex mechanism, whereby ADP-glucose binds to the enzyme before D-glucose 1-phosphate. GlgM shows no detecable glycogen synthase activity Mycolicibacterium smegmatis ATCC 700084 ?
-
 ?

Synonyms

Synonyms Comment Organism
glgM
-
 Mycolicibacterium smegmatis

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
40
-
-
 Mycolicibacterium smegmatis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6
-
-
 Mycolicibacterium smegmatis