Application | Comment | Organism |
---|---|---|
medicine | arylsulphatase AtsG , bifunctional glucosamine-1-phosphate acetyltransferase and N-acetylglucosamine-1-phosphate uridyl transferase GlmU and S-adenosyl-L-homocysteine hydrolase SahH are the Mycobacterium tuberculosis proteins that bind to human IL-8. The interactions with IL-8 are characterized by high binding affinity with KD values of 6.83x10-6 M, 5.24x10-6 M and 7.14x10-10 M, respectively. Strains overproducing the enzymes show a significantly increased number of intracellularly located bacilli compared with those of wild-type | Mycobacterium tuberculosis |
Cloned (Comment) | Organism |
---|---|
gene glmU, recombinant expression of His-tagged enzyme in Escherichia coli strain BL12(DE3) | Mycobacterium tuberculosis |
Protein Variants | Comment | Organism |
---|---|---|
additional information | construction of Mycobacterium tuberculosis mutant strains overproducing GlmU allows determination of the contribution of the protein to mycobacterial entry into human neutrophils | Mycobacterium tuberculosis |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
acetyl-CoA + alpha-D-glucosamine 1-phosphate | Mycobacterium tuberculosis | - |
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate | - |
? | |
acetyl-CoA + alpha-D-glucosamine 1-phosphate | Mycobacterium tuberculosis H37Rv | - |
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate | - |
? | |
acetyl-CoA + alpha-D-glucosamine 1-phosphate | Mycobacterium tuberculosis ATCC 25618 | - |
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Mycobacterium tuberculosis | P9WMN3 | - |
- |
Mycobacterium tuberculosis ATCC 25618 | P9WMN3 | - |
- |
Mycobacterium tuberculosis H37Rv | P9WMN3 | - |
- |
Purification (Comment) | Organism |
---|---|
recombinant His-tagged enzyme from Escherichia coli strain BL12(DE3) by cobalt affinity chromatography, overexpression of GlmU in Mycobacterium tuberculosis | Mycobacterium tuberculosis |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
acetyl-CoA + alpha-D-glucosamine 1-phosphate | - |
Mycobacterium tuberculosis | CoA + N-acetyl-alpha-D-glucosamine 1-phosphate | - |
? | |
acetyl-CoA + alpha-D-glucosamine 1-phosphate | - |
Mycobacterium tuberculosis H37Rv | CoA + N-acetyl-alpha-D-glucosamine 1-phosphate | - |
? | |
acetyl-CoA + alpha-D-glucosamine 1-phosphate | - |
Mycobacterium tuberculosis ATCC 25618 | CoA + N-acetyl-alpha-D-glucosamine 1-phosphate | - |
? | |
additional information | the recombinant enzyme binds to human interleukin-8, interaction analysis with human neutrophils, overview | Mycobacterium tuberculosis | ? | - |
? | |
additional information | the recombinant enzyme binds to human interleukin-8, interaction analysis with human neutrophils, overview | Mycobacterium tuberculosis H37Rv | ? | - |
? | |
additional information | the recombinant enzyme binds to human interleukin-8, interaction analysis with human neutrophils, overview | Mycobacterium tuberculosis ATCC 25618 | ? | - |
? |
Synonyms | Comment | Organism |
---|---|---|
GlmU | - |
Mycobacterium tuberculosis |
glucosamine-1-phosphate acetyltransferase | - |
Mycobacterium tuberculosis |
Rv1018c | - |
Mycobacterium tuberculosis |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
acetyl-CoA | - |
Mycobacterium tuberculosis |
General Information | Comment | Organism |
---|---|---|
physiological function | the enzyme is one of the pathogen proteins that bind to human interleukin-8, IL-8. The binding interaction of mycobacterial proteins AtsG, GlmU and SahH with human IL-8 may indicate that these proteins participate in the modulation of the early events of infection with tubercle bacilli and could affect pathogen attachment to target cells. Interleukin-8 belongs to the family of CXC chemokines and functions as a chemoattractant and activator of different subsets of leukocytes | Mycobacterium tuberculosis |