Enzymes
| UniProtKB help_outline | 4,978 proteins |
| Enzyme class help_outline |
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| GO Molecular Function help_outline |
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- Name help_outline allantoate Identifier CHEBI:17536 Charge -1 Formula C4H7N4O4 InChIKeyhelp_outline NUCLJNSWZCHRKL-UHFFFAOYSA-M SMILEShelp_outline NC(=O)NC(NC(N)=O)C([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 6 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline H2O Identifier CHEBI:15377 (Beilstein: 3587155; CAS: 7732-18-5) help_outline Charge 0 Formula H2O InChIKeyhelp_outline XLYOFNOQVPJJNP-UHFFFAOYSA-N SMILEShelp_outline [H]O[H] 2D coordinates Mol file for the small molecule Search links Involved in 6,204 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline (S)-ureidoglycolate Identifier CHEBI:57296 Charge -1 Formula C3H5N2O4 InChIKeyhelp_outline NWZYYCVIOKVTII-SFOWXEAESA-M SMILEShelp_outline NC(=O)N[C@@H](O)C([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 7 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline urea Identifier CHEBI:16199 (Beilstein: 635724; CAS: 57-13-6) help_outline Charge 0 Formula CH4N2O InChIKeyhelp_outline XSQUKJJJFZCRTK-UHFFFAOYSA-N SMILEShelp_outline NC(N)=O 2D coordinates Mol file for the small molecule Search links Involved in 25 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:11016 | RHEA:11017 | RHEA:11018 | RHEA:11019 | |
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| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
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Publications
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Hydrolysis, racemization and absolute configuration of ureidoglycolate, a substrate of allantoicase.
Gravenmade E.J., Vogels G.D., Van der Drift C.
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Crystal structure of yeast allantoicase reveals a repeated jelly roll motif.
Leulliot N., Quevillon-Cheruel S., Sorel I., Graille M., Meyer P., Liger D., Blondeau K., Janin J., van Tilbeurgh H.
Allantoicase (EC 3.5.3.4) catalyzes the conversion of allantoate into ureidoglycolate and urea, one of the final steps in the degradation of purines to urea. The mechanism of most enzymes involved in this pathway, which has been known for a long time, is unknown. In this paper we describe the thre ... >> More
Allantoicase (EC 3.5.3.4) catalyzes the conversion of allantoate into ureidoglycolate and urea, one of the final steps in the degradation of purines to urea. The mechanism of most enzymes involved in this pathway, which has been known for a long time, is unknown. In this paper we describe the three-dimensional crystal structure of the yeast allantoicase determined at a resolution of 2.6 A by single anomalous diffraction. This constitutes the first structure for an enzyme of this pathway. The structure reveals a repeated jelly roll beta-sheet motif, also present in proteins of unrelated biochemical function. Allantoicase has a hexameric arrangement in the crystal (dimer of trimers). Analysis of the protein sequence against the structural data reveals the presence of two totally conserved surface patches, one on each jelly roll motif. The hexameric packing concentrates these patches into conserved pockets that probably constitute the active site. << Less
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Crystal structure of an allantoicase (YIR029W) from Saccharomyces cerevisiae at 2.4 A resolution.
Xu Q., Schwarzenbacher R., Page R., Sims E., Abdubek P., Ambing E., Biorac T., Brinen L.S., Cambell J., Canaves J.M., Chiu H.J., Dai X., Deacon A.M., DiDonato M., Elsliger M.-A., Floyd R., Godzik A., Grittini C., Grzechnik S.K., Hampton E., Jaroszewski L., Karlak C., Klock H.E., Koesema E., Kovarik J.S., Kreusch A., Kuhn P., Lesley S.A., Levin I., McMullan D., McPhillips T.M., Miller M.D., Morse A., Moy K., Ouyang J., Quijano K., Reyes R., Rezezadeh F., Robb A., Spraggon G., Stevens R.C., van den Bedem H., Velasquez J., Vincent J., von Delft F., Wang X., West B., Wolf G., Hodgson K.O., Wooley J., Wilson I.A.