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Literature summary for 2.4.1.18 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 PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Mycobacterium tuberculosis

Crystallization (Commentary)

Crystallization (Comment) Organism
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

Protein Variants Comment Organism
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

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

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
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

Organism UniProt Comment Textmining
Mycobacterium tuberculosis P9WN45
-
-
Mycobacterium tuberculosis H37Rv P9WN45
-
-

Specific Activity [micromol/min/mg]

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

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
amylose
-
Mycobacterium tuberculosis amylose containing alpha-1,6-glucosidic linkages
-
?
amylose
-
Mycobacterium tuberculosis H37Rv amylose containing alpha-1,6-glucosidic linkages
-
?
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 ?
-
?
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 ?
-
?
starch
-
Mycobacterium tuberculosis starch containing alpha-1,6-glucosidic linkages
-
?
starch
-
Mycobacterium tuberculosis H37Rv starch containing alpha-1,6-glucosidic linkages
-
?

Synonyms

Synonyms Comment Organism
GlgB
-
Mycobacterium tuberculosis

Turnover Number [1/s]

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