EC number:3.5.3.1
Enzyme
Download| EC Tree |
| 3. Hydrolases |
| 3.5 Acting on carbon-nitrogen bonds, other than peptide bonds |
| 3.5.3 In linear amidines |
3D structure
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5CEV;
4CEV;
3CEV;
2CEV;
1CEV;
5RLA;
4RLA;
3RLA;
3E9B;
3E8Z;
3E8Q;
2RLA;
1ZPG;
1ZPE;
1TBL;
1TBJ;
1TBH;
1TA1;
1T5G;
1T5F;
1T4T;
1T4R;
1T4P;
1RLA;
1R1O;
1P8S;
1P8Q;
1P8P;
1P8O;
1P8N;
1P8M;
1HQX;
1HQH;
1HQG;
1HQF;
1P8R;
1HQ5;
1D3V;
1XFK;
1PQ3;
4IXV;
4IXU;
4IE3;
4IE2;
4I06;
4HZE;
1GQ7;
1GQ6;
4IE1;
4HXQ;
4HWW;
4GWD;
4GWC;
4GSZ;
4GSV;
4GSM;
4FCK;
4FCI;
3THJ;
3THH;
3THE;
3TH7;
3TF3;
3SKK;
3SJT;
3MJL;
3MFW;
3MFV;
3LP7;
3LP4;
3KV2;
3GN0;
3GMZ;
3F80;
3E6V;
3E6K;
3DJ8;
2ZAV;
2PLL;
2PHO;
2PHA;
2AEB;
1WVB;
1WVA;
6NFP;
6DKT;
3NIQ;
3NIP;
3NIO;
3M1R;
1T4S;
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References
External Links
| UniProtKB Enzyme Link: | UniProtKB 3.5.3.1 |
| BRENDA Enzyme Link: | BRENDA 3.5.3.1 |
| KEGG Enzyme Link: | KEGG3.5.3.1 |
| BioCyc Enzyme Link: | BioCyc 3.5.3.1 |
| ExPASy Enzyme Link: | ExPASy3.5.3.1 |
| EC2PDB Enzyme Link: | EC2PDB 3.5.3.1 |
| ExplorEnz Enzyme Link: | ExplorEnz 3.5.3.1 |
| PRIAM enzyme-specific profiles Link: | PRIAM 3.5.3.1 |
| IntEnz Enzyme Link: | IntEnz 3.5.3.1 |
| MEDLINE Enzyme Link: | MEDLINE 3.5.3.1 |
| RHEA:20569 | H2O + L-arginine = L-ornithine + urea |
| RULE(radius=1) | [*:1]-[C;H0;+0:2](=[NH;+0:3])-[NH;+0:4]-[*:5].[OH2;+0:6]>>[*:1]-[C;H0;+0:2](-[NH2;+0:3])=[O;H0;+0:6].[*:5]-[NH2;+0:4] |
| Reaction |  |
| Core-to-Core | No scaffolds atoms were exchanged as a result of the reaction |
References
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| Structure of a unique binuclear manganese cluster in arginase. | Kanyo ZF, Scolnick LR, Ash DE, Christianson DW | 1996 Oct 10 | 8849731 |
| Arginase: structure, mechanism, and physiological role in male and female sexual arousal. | Christianson DW | 2005 Mar | 15766238 |
| Structure and function of arginases. | Ash DE | 2004 Oct | 15465781 |
| Arginase: a binuclear manganese metalloenzyme. | Ash DE, Cox JD, Christianson DW | 2000 | 10693141 |