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*Now available with Java™ 1.5!*
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| Family: |
L-ASPARAGINASE (PTHR11707)
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| Subfamilies: |
4
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| PANTHER Links: |
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| Abstract: |
Asparaginase, which is found in various plant, animal and bacterial cells, catalyses the deamination of asparagine to yield aspartic acid and an ammonium ion, resulting in a depletion of free circulatory asparagine in plasma [PMID:3026924]. The enzyme is effective in the treatment of human malignant lymphomas, which have a diminished capacity to produce asparagine synthetase: in order to survive, such cells absorb asparagine from blood plasma [PMID:2407723, PMID:3379033] - if Asn levels have been depleted by injection of asparaginase, the lymphoma cells die. Glutaminase, a similar enzyme, catalyses the deaminination of glutamine to glutamic acid and an ammonium ion [PMID:2407723]. Both enzymes are homotetramers [PMID:3026924]: two threonine residues in the N-terminal half of the proteins are involved in the catalytic activity.
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| InterPro Accession: |
IPR006034
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| PANTHER Molecular Function: |
Molecular function unclassified
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| PANTHER Biological Process: |
Biological process unclassified
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| Pathway Categories: |
No pathway information available
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| Training Sequences: |
33
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| HMM Length |
422
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| Downloads: |
HMM (HMMER format) |
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Total |
Celera |
FlyBase |
NCBI |
| H. sapiens |
2
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1
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0 |
1
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| M. musculus |
2
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1
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0 |
1
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| R. norvegicus |
2
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1
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0 |
1
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| D. melanogaster |
2
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0 |
2
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0 |
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