Enzymes
| UniProtKB help_outline | 187 proteins |
Reaction participants Show >> << Hide
- Name help_outline taurocyamine Identifier CHEBI:58064 Charge 0 Formula C3H9N3O3S InChIKeyhelp_outline JKLRIMRKZBSSED-UHFFFAOYSA-N SMILEShelp_outline NC(=[NH2+])NCCS([O-])(=O)=O 2D coordinates Mol file for the small molecule Search links Involved in 3 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline H2O Identifier CHEBI:15377 (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 6,485 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline urea Identifier CHEBI:16199 (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
- Name help_outline taurine Identifier CHEBI:507393 Charge 0 Formula C2H7NO3S InChIKeyhelp_outline XOAAWQZATWQOTB-UHFFFAOYSA-N SMILEShelp_outline [NH3+]CCS([O-])(=O)=O 2D coordinates Mol file for the small molecule Search links Involved in 46 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:75931 | RHEA:75932 | RHEA:75933 | RHEA:75934 | |
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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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Guanidino acid hydrolysis by the human enzyme annotated as agmatinase.
Sinn M., Stanoppi M., Hauth F., Fleming J.R., Funck D., Mayans O., Hartig J.S.
Guanidino acids such as taurocyamine, guanidinobutyrate, guanidinopropionate, and guanidinoacetate have been detected in humans. However, except for guanidionacetate, which is a precursor of creatine, their metabolism and potential functions remain poorly understood. Agmatine has received consider ... >> More
Guanidino acids such as taurocyamine, guanidinobutyrate, guanidinopropionate, and guanidinoacetate have been detected in humans. However, except for guanidionacetate, which is a precursor of creatine, their metabolism and potential functions remain poorly understood. Agmatine has received considerable attention as a potential neurotransmitter and the human enzyme so far annotated as agmatinase (AGMAT) has been proposed as an important modulator of agmatine levels. However, conclusive evidence for the assigned enzymatic activity is lacking. Here we show that AGMAT hydrolyzed a range of linear guanidino acids but was virtually inactive with agmatine. Structural modelling and direct biochemical assays indicated that two naturally occurring variants differ in their substrate preferences. A negatively charged group in the substrate at the end opposing the guanidine moiety was essential for efficient catalysis, explaining why agmatine was not hydrolyzed. We suggest to rename AGMAT as guanidino acid hydrolase (GDAH). Additionally, we demonstrate that the GDAH substrates taurocyamine, guanidinobutyrate and guanidinopropionate were produced by human glycine amidinotransferase (GATM). The presented findings show for the first time an enzymatic activity for GDAH/AGMAT. Since agmatine has frequently been proposed as an endogenous neurotransmitter, the current findings clarify important aspects of the metabolism of agmatine and guanidino acid derivatives in humans. << Less
Sci. Rep. 12:22088-22088(2022) [PubMed] [EuropePMC]
This publication is cited by 6 other entries.