Enzymes
| UniProtKB help_outline | 4 proteins |
| Enzyme class help_outline |
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- Name help_outline oxamate Identifier CHEBI:58363 (Beilstein: 3903880) help_outline Charge -1 Formula C2H2NO3 InChIKeyhelp_outline SOWBFZRMHSNYGE-UHFFFAOYSA-M SMILEShelp_outline NC(=O)C([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 2 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline carbamoyl phosphate Identifier CHEBI:58228 (CAS: 63082-13-3) help_outline Charge -2 Formula CH2NO5P InChIKeyhelp_outline FFQKYPRQEYGKAF-UHFFFAOYSA-L SMILEShelp_outline NC(=O)OP([O-])([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 17 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline N-carbamoyl-2-oxoglycine Identifier CHEBI:57824 (Beilstein: 3905016) help_outline Charge -1 Formula C3H3N2O4 InChIKeyhelp_outline UWBHMRBRLOJJAA-UHFFFAOYSA-M SMILEShelp_outline NC(=O)NC(=O)C([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 4 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline phosphate Identifier CHEBI:43474 Charge -2 Formula HO4P InChIKeyhelp_outline NBIIXXVUZAFLBC-UHFFFAOYSA-L SMILEShelp_outline OP([O-])([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 1,020 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:22984 | RHEA:22985 | RHEA:22986 | RHEA:22987 | |
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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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OXAMIC TRANSCARBAMYLASE OF STREPTOCOCCUS ALLANTOICUS.
BOJANOWSKI R., GAUDY E., VALENTINE R.C., WOLFE R.S.
Bojanowski, R. (University of Illinois, Urbana), Elizabeth Gaudy, R. C. Valentine, and R. S. Wolfe. Oxamic transcarbamylase of Streptococcus allantoicus. J. Bacteriol. 87:75-80. 1964.-An improved colorimetric assay for carbamyl oxamate, which allows the precise measurement of the activity of oxami ... >> More
Bojanowski, R. (University of Illinois, Urbana), Elizabeth Gaudy, R. C. Valentine, and R. S. Wolfe. Oxamic transcarbamylase of Streptococcus allantoicus. J. Bacteriol. 87:75-80. 1964.-An improved colorimetric assay for carbamyl oxamate, which allows the precise measurement of the activity of oxamic transcarbamylase, has been developed. Activity is maximum over the pH range from 8.3 to 8.7. A cation requirement is satisfied by 2.5 x 10(-3)m Mg(++) or Mn(++). The equilibrium constant for the phosphorolysis of carbamyl oxamic acid is 1.6, corresponding to a negative free energy change of -285 cal per mole. << Less
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Phosphorolysis of carbamyl oxamic acid.
VALENTINE R.C., WOLFE R.S.
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Oxamic transcarbamylase of Escherichia coli is encoded by the three genes allFGH (formerly fdrA, ylbE, and ylbF).
Kim N.Y., Kim O.B.
<i>Escherichia coli</i> uses allantoin as the sole nitrogen source during anaerobic growth. In the final step of allantoin degradation, oxamic transcarbamylase (OXTCase) converts oxalurate to carbamoyl phosphate (CP) and oxamate. The activity of this enzyme was first measured in <i>Streptococcus a ... >> More
<i>Escherichia coli</i> uses allantoin as the sole nitrogen source during anaerobic growth. In the final step of allantoin degradation, oxamic transcarbamylase (OXTCase) converts oxalurate to carbamoyl phosphate (CP) and oxamate. The activity of this enzyme was first measured in <i>Streptococcus allantoicus</i> in the 1960s, but no OXTCase enzyme or the encoding gene(s) have been found in any strain. This study discovered that <i>allFGH</i> (<i>fdrA</i>, <i>ylbE</i>, and <i>ylbF</i>) are the genes that encode the global orphan enzyme OXTCase. The three genes form an operon together with <i>allK</i> (<i>ybcF</i>), encoding catabolic carbamate kinase. The <i>allFGHK</i> operon is located directly downstream of the <i>allECD</i> operon that encodes enzymes for the preceding steps of OXTCase. The OXTCase kinetic parameters were analyzed using the purified protein composed of AllF-AllG-AllH (FdrA-YlbE-YlbF); for the substrate CP, <i>K</i><sub><i>M</i></sub> and <i>V</i><sub>max</sub> were 1.3 mM and 15.4 U/mg OXTCase, respectively, and for the substrate oxamate, they were 36.9 mM and 27.0 U/mg OXTCase. In addition, the OXTCase encoded by the three genes is a novel transcarbamylase that shows no similarity with known enzymes of the transcarbamylase family such as aspartate transcarbamylase, ornithine transcarbamylase, and YgeW transcarbamylase. The present study elucidated the anaerobic allantoin degradation pathway of <i>E. coli</i>. Therefore, we suggest that the genes <i>fdrA</i>, <i>ylbE</i>, and <i>ylbF</i> are renamed <i>allF</i>, <i>allG</i>, and <i>allH</i>, respectively.IMPORTANCEThe anaerobic allantoin degradation pathway of <i>Escherichia coli</i> includes a global orphan enzyme, oxamic transcarbamylase (OXTCase), which converts oxalurate to carbamoyl phosphate and oxamate. This study found that the <i>allFGH</i> (<i>fdrA</i>, <i>ylbE</i>, and <i>ylbF</i>) genes encode OXTCase. The OXTCase activity and kinetics were successfully determined with purified recombinant AllF-AllG-AllH (FdrA-YlbE-YlbF). This OXTCase is a novel transcarbamylase that shows no similarity with known enzymes of the transcarbamylase family such as aspartate transcarbamylase (ATCase), ornithine transcarbamylase (OTCase), and YgeW transcarbamylase (YTCase). In addition, OXTCase activity requires three genes, whereas ATCase is encoded by two genes, and OTCase and YTCase are encoded by a single gene. The current study discovered OXTCase, the last unknown step in allantoin degradation, and this enzyme is a new member of the transcarbamylase group that was previously unknown. << Less
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INDUCTION OF CARBAMYL-P SPECIFIC OXAMATE TRANSCARBAMYLASE BY PARABANIC ACID IN A STREPTOCOCCUS.
TIGIER H., GRISOLIA S.
Biochem Biophys Res Commun 19:209-214(1965) [PubMed] [EuropePMC]
Comments
N-carbamoyl-2-oxoglycine == oxalurate