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Literature summary extracted from

  • Garg, S.K.; Alam, M.S.; Kishan, K.V.; Agrawal, P.
    Expression and characterization of alpha-(1,4)-glucan branching enzyme Rv1326c of Mycobacterium tuberculosis H37Rv (2007), Protein Expr. Purif., 51, 198-208.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.4.1.18 expressed in Escherichia coli DG5alpha Mycobacterium tuberculosis

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.4.1.18 Ca2+ the cation has no effect on the activity. The reaction mixture is incubated in the presence of 10 mM of the cation for 30 min Mycobacterium tuberculosis
2.4.1.18 Cu2+ maximum inhibition is observed, where about 40% of the activity is retained. The reaction mixture is incubated in the presence of 10 mM of the cation for 30 min Mycobacterium tuberculosis
2.4.1.18 Mg2+ the cation has no effect on the activity. The reaction mixture is incubated in the presence of 10 mM of the cation for 30 min Mycobacterium tuberculosis
2.4.1.18 Zn2+ about 70% activity retained. The reaction mixture is incubated in the presence of 10 mM of the cation for 30 min Mycobacterium tuberculosis

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.4.1.18 80000
-
 gel filtration chromatography using Superdex 200 HR10/30 column Mycobacterium tuberculosis
2.4.1.18 85000
-
 SDS-PAGE at 4°C Mycobacterium tuberculosis
2.4.1.18 86060
-
 theoretical mass of the recombinant branching enzyme with N-terminal S-tag and C-terminal His-tag Mycobacterium tuberculosis

Organism

EC Number Organism UniProt Comment Textmining
2.4.1.18 Mycobacterium tuberculosis P9WN45 the primary amino acid sequence has four cysteine residues at position: 95, 193, 617 and 658, therefore there is a possibility of forming intramoleculare disulfide bonds. The two closely migrating bands of purified protein on a non-reducing SDS-PAGE might be due to the presence of two populations of different confomations of the same protein: the oxidized and the reduced.; H37Rv
-
2.4.1.18 Mycobacterium tuberculosis H37Rv P9WN45 the primary amino acid sequence has four cysteine residues at position: 95, 193, 617 and 658, therefore there is a possibility of forming intramoleculare disulfide bonds. The two closely migrating bands of purified protein on a non-reducing SDS-PAGE might be due to the presence of two populations of different confomations of the same protein: the oxidized and the reduced.; H37Rv
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.4.1.18 Ni2+-NTA affinity column and Q-Sepharose column Mycobacterium tuberculosis

Synonyms

EC Number Synonyms Comment Organism
2.4.1.18 GlgB glycogen branching enzyme Mycobacterium tuberculosis
2.4.1.18 ORF Rv1326c in Mycobacterium tuberculosis H37Rv codes for a enzymatically active protein that utilizes amylose as the substrate Mycobacterium tuberculosis

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.4.1.18 30
-
 incubated at different temperatures for 30 min at pH 7 in 50 mM citrate buffer Mycobacterium tuberculosis

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
2.4.1.18 10 30 pre-incubation of the enzyme for 2 h at different temperatures, following enzyme assay is conducted at 30°C. About 80% activity is retained after pre-incubation at 37°C and 45°C Mycobacterium tuberculosis
2.4.1.18 45
-
 with a direct enzyme assay at 45°C the enzyme retains about 45% activity Mycobacterium tuberculosis

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.4.1.18 7
-
 all assays are perfomed at 30°C with 0.5 microM of protein Mycobacterium tuberculosis