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Literature summary extracted from

  • Pal, K.; Kumar, S.; Sharma, S.; Garg, S.K.; Alam, M.S.; Xu, H.E.; Agrawal, P.; Swaminathan, K.
    Crystal structure of full-length Mycobacterium tuberculosis H37Rv glycogen branching enzyme: insights of N-terminal beta-sandwich in substrate specificity and enzymatic activity (2010), J. Biol. Chem., 285, 20897-20903.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.4.1.18 expression in Escherichia coli Mycobacterium tuberculosis

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.4.1.18 crystal structure of full-length protein at 2.33 A resolution. The enzyme contains four domains: N1 beta-sandwich, N2 beta-sandwich, a central (beta/alpha)8 domain that houses the catalytic site, and a C-terminal beta-sandwich. The N1 beta-sandwich, which is formed by the first 105 amino acids and superimposes well with the N2 beta-sandwich, has an influence in substrate binding in the amylase assay Mycobacterium tuberculosis

Protein Variants

EC Number Protein Variants Comment Organism
2.4.1.18 additional information a mutant lacking the N1 domain, i.e. lacking N-terminal residues 1-108, shows about 30% decrease in specific activity Mycobacterium tuberculosis

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.4.1.18 additional information not inhibitory: ADP, ADP glucose, tunicamycin, castenospermine, nojirimycin, or acarbose Mycobacterium tuberculosis

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.4.1.18 additional information
-
 additional information Km-value for amylose is 0.56 mg/ml, wild-type, 25°C, pH 7.0. Km value for mutant lacking N1 domain is 0.33 mg/ml Mycobacterium tuberculosis

Organism

EC Number Organism UniProt Comment Textmining
2.4.1.18 Mycobacterium tuberculosis P9WN45
-
-
2.4.1.18 Mycobacterium tuberculosis H37Rv P9WN45
-
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
2.4.1.18 42
-
 mutant lacking the N1 domain, i.e. lacking N-terminal residues 1-108, pH 7.0, 25°C Mycobacterium tuberculosis
2.4.1.18 63.75
-
 wild-type, pH 7.0, 25°C Mycobacterium tuberculosis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.4.1.18 amylose
-
 Mycobacterium tuberculosis amylose containing alpha-1,6-glucosidic linkages
-
 ?
2.4.1.18 amylose
-
 Mycobacterium tuberculosis H37Rv amylose containing alpha-1,6-glucosidic linkages
-
 ?
2.4.1.18 additional information two-step reaction mechanism for the amylase activity, i.e. 1-4 bond breakage, and isomerization, i.e. 1-6 bond formation, which occur in the same catalytic pocket Mycobacterium tuberculosis ?
-
 ?
2.4.1.18 additional information two-step reaction mechanism for the amylase activity, i.e. 1-4 bond breakage, and isomerization, i.e. 1-6 bond formation, which occur in the same catalytic pocket Mycobacterium tuberculosis H37Rv ?
-
 ?
2.4.1.18 starch
-
 Mycobacterium tuberculosis starch containing alpha-1,6-glucosidic linkages
-
 ?
2.4.1.18 starch
-
 Mycobacterium tuberculosis H37Rv starch containing alpha-1,6-glucosidic linkages
-
 ?

Synonyms

EC Number Synonyms Comment Organism
2.4.1.18 GlgB
-
 Mycobacterium tuberculosis

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2.4.1.18 0.068
-
 amylose mutant lacking N1 domain, pH 7.0, 25°C Mycobacterium tuberculosis
2.4.1.18 0.15
-
 amylose wild-type, pH 7.0, 25°C Mycobacterium tuberculosis