EC number:3.5.1.38
Enzyme
Download| EC Tree |
| 3. Hydrolases |
| 3.5 Acting on carbon-nitrogen bonds, other than peptide bonds |
| 3.5.1 In linear amides |
| ID: | 3.5.1.38 | ||
|---|---|---|---|
| Description: | Glutamin-(asparagin-)ase. | ||
| Alternative Name: |
L-asparagine/L-glutamine amidohydrolase. L-ASNase/L-GLNase. Glutaminase-asparaginase. | ||
| Prosite: | PDOC00132; | ||
| PDB: |
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| Cath: | 3.40.50.40; 3.40.50.1170; |
3D structure
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External Links
| UniProtKB Enzyme Link: | UniProtKB 3.5.1.38 |
| BRENDA Enzyme Link: | BRENDA 3.5.1.38 |
| KEGG Enzyme Link: | KEGG3.5.1.38 |
| BioCyc Enzyme Link: | BioCyc 3.5.1.38 |
| ExPASy Enzyme Link: | ExPASy3.5.1.38 |
| EC2PDB Enzyme Link: | EC2PDB 3.5.1.38 |
| ExplorEnz Enzyme Link: | ExplorEnz 3.5.1.38 |
| PRIAM enzyme-specific profiles Link: | PRIAM 3.5.1.38 |
| IntEnz Enzyme Link: | IntEnz 3.5.1.38 |
| MEDLINE Enzyme Link: | MEDLINE 3.5.1.38 |
| RHEA:21016 | H2O + L-asparagine = L-aspartate + NH4(+) |
| RULE(radius=1) | [*:1]-[C;H0;+0:2](=[*:3])-[NH2;+0:4].[OH2;+0:5]>>[*:1]-[C;H0;+0:2](=[*:3])-[OH;+0:5].[NH3;+0:4] |
| Reaction |  |
| Core-to-Core | No scaffolds atoms were exchanged as a result of the reaction |
References
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| Cloning and expression of cDNA encoding rat liver 60-kDa lysophospholipase containing an asparaginase-like region and ankyrin repeat. | Sugimoto H, Odani S, Yamashita S | 1998 May 15 | 9575212 |
| Structural characterization of Pseudomonas 7A glutaminase-asparaginase. | Lubkowski J, Wlodawer A, Ammon HL, Copeland TD, Swain AL | 1994 Aug 30 | 8068664 |
| Structures of amidohydrolases. Amino acid sequence of a glutaminase-asparaginase from Acinetobacter glutaminasificans and preliminary crystallographic data for an asparaginase from Erwinia chrysanthemi. | Tanaka S, Robinson EA, Appella E, Miller M, Ammon HL, Roberts J, Weber IT, Wlodawer A | 1988 Jun 25 | 3379033 |
| Uncoupling intramolecular processing and substrate hydrolysis in the N-terminal nucleophile hydrolase hASRGL1 by circular permutation. | Li W, Cantor JR, Yogesha SD, Yang S, Chantranupong L, Liu JQ, Agnello G, Georgiou G, Stone EM, Zhang Y | 2012 Nov 16 | 22891768 |
| The human asparaginase-like protein 1 hASRGL1 is an Ntn hydrolase with beta-aspartyl peptidase activity. | Cantor JR, Stone EM, Chantranupong L, Georgiou G | 2009 Nov 24 | 19839645 |
| Crystal structure and allosteric regulation of the cytoplasmic Escherichia coli L-asparaginase I. | Yun MK, Nourse A, White SW, Rock CO, Heath RJ | 2007 Jun 8 | 17451745 |
| Gliap--a novel untypical L-asparaginase localized to rat brain astrocytes. | Dieterich DC, Landwehr M, Reissner C, Smalla KH, Richter K, Wolf G, Böckers TM, Gundelfinger ED, Kreutz MR | 2003 Jun | 12753071 |
| Reactions of Pseudomonas 7A glutaminase-asparaginase with diazo analogues of glutamine and asparagine result in unexpected covalent inhibitions and suggests an unusual catalytic triad Thr-Tyr-Glu. | Ortlund E, Lacount MW, Lewinski K, Lebioda L | 2000 Feb 15 | 10684596 |
| RHEA:15889 | H2O + L-glutamine = L-glutamate + NH4(+) |
| RULE(radius=1) | [*:1]-[C;H0;+0:2](=[*:3])-[NH2;+0:4].[OH2;+0:5]>>[*:1]-[C;H0;+0:2](=[*:3])-[OH;+0:5].[NH3;+0:4] |
| Reaction |  |
| Core-to-Core | No scaffolds atoms were exchanged as a result of the reaction |
References
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| Gamma-glutamylmethylamide. A new intermediate in the metabolism of methylamine. | Kung HF, Wagner C | 1969 Aug 10 | 5800436 |