Details
| Stereochemistry | ACHIRAL |
| Molecular Formula | C3H5NO2 |
| Molecular Weight | 87.0773 |
| Optical Activity | NONE |
| Defined Stereocenters | 0 / 0 |
| E/Z Centers | 0 |
| Charge | 0 |
SHOW SMILES / InChI
SMILES
CC(=O)C(N)=O
InChI
InChIKey=FPOLWERNILTNDK-UHFFFAOYSA-N
InChI=1S/C3H5NO2/c1-2(5)3(4)6/h1H3,(H2,4,6)
| Molecular Formula | C3H5NO2 |
| Molecular Weight | 87.0773 |
| Charge | 0 |
| Count |
|
| Stereochemistry | ACHIRAL |
| Additional Stereochemistry | No |
| Defined Stereocenters | 0 / 0 |
| E/Z Centers | 0 |
| Optical Activity | NONE |
Approval Year
PubMed
| Title | Date | PubMed |
|---|---|---|
| Structural insights into the prereaction state of pyruvate decarboxylase from Zymomonas mobilis . | 2010-03-02 |
|
| A novel 4-oxo-2(E)-nonenal-derived modification to angiotensin II: oxidative decarboxylation of N-terminal aspartic acid. | 2008-12 |
|
| Function of a conserved loop of the beta-domain, not involved in thiamin diphosphate binding, in catalysis and substrate activation in yeast pyruvate decarboxylase. | 2006-11-14 |
|
| The crystal structure of pyruvate decarboxylase from Kluyveromyces lactis. Implications for the substrate activation mechanism of this enzyme. | 2006-09 |
|
| N-terminal protein modification through a biomimetic transamination reaction. | 2006-08-11 |
|
| Interaction of thiamin diphosphate with phosphorylated and dephosphorylated mammalian pyruvate dehydrogenase complex. | 2005-01 |
|
| Pyruvate decarboxylase from Kluyveromyces lactis. An enzyme with an extraordinary substrate activation behaviour. | 2002-07 |
|
| Spectroscopic evidence for participation of the 1',4'-imino tautomer of thiamin diphosphate in catalysis by yeast pyruvate decarboxylase. | 2002-06 |
|
| New model for activation of yeast pyruvate decarboxylase by substrate consistent with the alternating sites mechanism: demonstration of the existence of two active forms of the enzyme. | 2002-03-26 |
|
| Catalytic acid-base groups in yeast pyruvate decarboxylase. 3. A steady-state kinetic model consistent with the behavior of both wild-type and variant enzymes at all relevant pH values. | 2001-06-26 |
| Substance Class |
Chemical
Created
by
admin
on
Edited
Mon Mar 31 20:10:05 GMT 2025
by
admin
on
Mon Mar 31 20:10:05 GMT 2025
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| Record UNII |
P4O9E1R444
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| Record Status |
Validated (UNII)
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| Record Version |
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