Cloned (Comment) | Organism |
---|---|
expression in Escherichia coli | Mycobacterium tuberculosis |
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 | 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 | Comment | Organism | Structure |
---|---|---|---|
additional information | not inhibitory: ADP, ADP glucose, tunicamycin, castenospermine, nojirimycin, or acarbose | Mycobacterium tuberculosis |
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 | UniProt | Comment | Textmining |
---|---|---|---|
Mycobacterium tuberculosis | P9WN45 | - |
- |
Mycobacterium tuberculosis H37Rv | P9WN45 | - |
- |
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 | 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 | Comment | Organism |
---|---|---|
GlgB | - |
Mycobacterium tuberculosis |
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 |