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Literature summary 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 PubMedView publication on EuropePMC

Crystallization (Commentary)

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

Inhibitors

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

Organism

EC Number Organism UniProt Comment Textmining
2.4.1.342 Mycolicibacterium smegmatis A0R2E2
-
-
2.4.1.342 Mycolicibacterium smegmatis ATCC 700084 A0R2E2
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-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.4.1.342 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 ?
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-
2.4.1.342 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

EC Number Synonyms Comment Organism
2.4.1.342 glgM
-
 Mycolicibacterium smegmatis

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.4.1.342 40
-
-
 Mycolicibacterium smegmatis

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.4.1.342 6
-
-
 Mycolicibacterium smegmatis