| + |
AMPK | up-regulates activity 
phosphorylation
|
CTH |
0.25 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277794 |
Ser346 |
ESLGGFEsLAELPAI |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 37922764 |
Here we define an important mechanism of increased persulfide and polysulfide production involving cystathionine gamma lyase (CSE) phosphorylation at serine 346 and threonine 355 in a substrate specific manner, under acute hypoxic conditions. Hypoxic phosphorylation of CSE occurs in an AMP kinase dependent manner increasing enzyme activity involving unique inter- and intramolecular interactions within the tetramer. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277808 |
Ser346 |
ESLGGFEsLAELPAI |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 37922764 |
Here we define an important mechanism of increased persulfide and polysulfide production involving cystathionine gamma lyase (CSE) phosphorylation at serine 346 and threonine 355 in a substrate specific manner, under acute hypoxic conditions. Hypoxic phosphorylation of CSE occurs in an AMP kinase dependent manner increasing enzyme activity involving unique inter- and intramolecular interactions within the tetramer. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277807 |
Thr355 |
AELPAIMtHASVLKN |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 37922764 |
Here we define an important mechanism of increased persulfide and polysulfide production involving cystathionine gamma lyase (CSE) phosphorylation at serine 346 and threonine 355 in a substrate specific manner, under acute hypoxic conditions. Hypoxic phosphorylation of CSE occurs in an AMP kinase dependent manner increasing enzyme activity involving unique inter- and intramolecular interactions within the tetramer. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277793 |
Thr355 |
AELPAIMtHASVLKN |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 37922764 |
Here we define an important mechanism of increased persulfide and polysulfide production involving cystathionine gamma lyase (CSE) phosphorylation at serine 346 and threonine 355 in a substrate specific manner, under acute hypoxic conditions. Hypoxic phosphorylation of CSE occurs in an AMP kinase dependent manner increasing enzyme activity involving unique inter- and intramolecular interactions within the tetramer. |
|
| Publications: |
4 |
Organism: |
Homo Sapiens |
| + |
PRKG2 | down-regulates activity 
phosphorylation
|
CTH |
0.244 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-275800 |
Ser377 |
SDTLIRLsVGLEDEE |
|
|
| pmid |
sentence |
| 25900831 |
CO stimulated protein kinase G (PKG)-dependent phosphorylation of Ser(377) of CSE, inhibiting the production of H2S. |
|
| Publications: |
1 |
| + |
CTH | up-regulates quantity
chemical modification
|
hydrosulfide |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-275819 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 19961860 |
the role of CSE in this reaction pathway is to convert l-cystathionine into l-cysteine whilst generating α-ketobutyrate and ammonia (Fig. 1). The reaction proceeds via an α,γ-elimination mechanism where the C–γ–S bond of l-cystathionine is specifically cleaved to yield l-cysteine.12 Defects in this metabolic pathway are associated with cystathioninuria, l-cysteine deficiency and subsequent impairment of glutathione metabolism, as well as higher plasma homocysteine concentrations.13, 14, 15, 16, 17 Besides its role in the conversion of l-cystathionine into l-cysteine, studies have also shown that CSE can utilize l-cysteine as a substrate for producing H2S via an α,β-elimination reaction (Fig. 1).18, 19, 20 However, to date, no reports have clearly demonstrated the residues that affect CSE-mediated H2S production. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
Kidney, Liver, Vascular Cell |
| + |
CTH | down-regulates quantity
chemical modification
|
L-selenocystathionine zwitterion |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-275823 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 19961860 |
the role of CSE in this reaction pathway is to convert l-cystathionine into l-cysteine whilst generating α-ketobutyrate and ammonia (Fig. 1). The reaction proceeds via an α,γ-elimination mechanism where the C–γ–S bond of l-cystathionine is specifically cleaved to yield l-cysteine.12 Defects in this metabolic pathway are associated with cystathioninuria, l-cysteine deficiency and subsequent impairment of glutathione metabolism, as well as higher plasma homocysteine concentrations.13, 14, 15, 16, 17 Besides its role in the conversion of l-cystathionine into l-cysteine, studies have also shown that CSE can utilize l-cysteine as a substrate for producing H2S via an α,β-elimination reaction (Fig. 1).18, 19, 20 However, to date, no reports have clearly demonstrated the residues that affect CSE-mediated H2S production. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
Kidney, Liver, Vascular Cell |
| + |
CTH | up-regulates quantity
chemical modification
|
L-selenocysteine zwitterion |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-275821 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 19961860 |
the role of CSE in this reaction pathway is to convert l-cystathionine into l-cysteine whilst generating α-ketobutyrate and ammonia (Fig. 1). The reaction proceeds via an α,γ-elimination mechanism where the C–γ–S bond of l-cystathionine is specifically cleaved to yield l-cysteine.12 Defects in this metabolic pathway are associated with cystathioninuria, l-cysteine deficiency and subsequent impairment of glutathione metabolism, as well as higher plasma homocysteine concentrations.13, 14, 15, 16, 17 Besides its role in the conversion of l-cystathionine into l-cysteine, studies have also shown that CSE can utilize l-cysteine as a substrate for producing H2S via an α,β-elimination reaction (Fig. 1).18, 19, 20 However, to date, no reports have clearly demonstrated the residues that affect CSE-mediated H2S production. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
Kidney, Liver, Vascular Cell |
| + |
CTH | up-regulates quantity
chemical modification
|
L-cysteine zwitterion |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-275818 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 19961860 |
the role of CSE in this reaction pathway is to convert l-cystathionine into l-cysteine whilst generating α-ketobutyrate and ammonia (Fig. 1). The reaction proceeds via an α,γ-elimination mechanism where the C–γ–S bond of l-cystathionine is specifically cleaved to yield l-cysteine.12 Defects in this metabolic pathway are associated with cystathioninuria, l-cysteine deficiency and subsequent impairment of glutathione metabolism, as well as higher plasma homocysteine concentrations.13, 14, 15, 16, 17 Besides its role in the conversion of l-cystathionine into l-cysteine, studies have also shown that CSE can utilize l-cysteine as a substrate for producing H2S via an α,β-elimination reaction (Fig. 1).18, 19, 20 However, to date, no reports have clearly demonstrated the residues that affect CSE-mediated H2S production. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
Kidney, Liver, Vascular Cell |
| + |
CTH | down-regulates quantity
chemical modification
|
L-homocysteine zwitterion |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-275825 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 19961860 |
the role of CSE in this reaction pathway is to convert l-cystathionine into l-cysteine whilst generating α-ketobutyrate and ammonia (Fig. 1). The reaction proceeds via an α,γ-elimination mechanism where the C–γ–S bond of l-cystathionine is specifically cleaved to yield l-cysteine.12 Defects in this metabolic pathway are associated with cystathioninuria, l-cysteine deficiency and subsequent impairment of glutathione metabolism, as well as higher plasma homocysteine concentrations.13, 14, 15, 16, 17 Besides its role in the conversion of l-cystathionine into l-cysteine, studies have also shown that CSE can utilize l-cysteine as a substrate for producing H2S via an α,β-elimination reaction (Fig. 1).18, 19, 20 However, to date, no reports have clearly demonstrated the residues that affect CSE-mediated H2S production. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
Kidney, Liver, Vascular Cell |
| + |
CTH | down-regulates quantity
chemical modification
|
L-cystathionine dizwitterion |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-275822 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 19961860 |
the role of CSE in this reaction pathway is to convert l-cystathionine into l-cysteine whilst generating α-ketobutyrate and ammonia (Fig. 1). The reaction proceeds via an α,γ-elimination mechanism where the C–γ–S bond of l-cystathionine is specifically cleaved to yield l-cysteine.12 Defects in this metabolic pathway are associated with cystathioninuria, l-cysteine deficiency and subsequent impairment of glutathione metabolism, as well as higher plasma homocysteine concentrations.13, 14, 15, 16, 17 Besides its role in the conversion of l-cystathionine into l-cysteine, studies have also shown that CSE can utilize l-cysteine as a substrate for producing H2S via an α,β-elimination reaction (Fig. 1).18, 19, 20 However, to date, no reports have clearly demonstrated the residues that affect CSE-mediated H2S production. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
Kidney, Liver, Vascular Cell |
| + |
CTH | up-regulates quantity
chemical modification
|
pyruvate |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-275820 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 19961860 |
the role of CSE in this reaction pathway is to convert l-cystathionine into l-cysteine whilst generating α-ketobutyrate and ammonia (Fig. 1). The reaction proceeds via an α,γ-elimination mechanism where the C–γ–S bond of l-cystathionine is specifically cleaved to yield l-cysteine.12 Defects in this metabolic pathway are associated with cystathioninuria, l-cysteine deficiency and subsequent impairment of glutathione metabolism, as well as higher plasma homocysteine concentrations.13, 14, 15, 16, 17 Besides its role in the conversion of l-cystathionine into l-cysteine, studies have also shown that CSE can utilize l-cysteine as a substrate for producing H2S via an α,β-elimination reaction (Fig. 1).18, 19, 20 However, to date, no reports have clearly demonstrated the residues that affect CSE-mediated H2S production. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
Kidney, Liver, Vascular Cell |
| + |
CTH | down-regulates quantity
chemical modification
|
L-cysteine zwitterion |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-275824 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 19961860 |
the role of CSE in this reaction pathway is to convert l-cystathionine into l-cysteine whilst generating α-ketobutyrate and ammonia (Fig. 1). The reaction proceeds via an α,γ-elimination mechanism where the C–γ–S bond of l-cystathionine is specifically cleaved to yield l-cysteine.12 Defects in this metabolic pathway are associated with cystathioninuria, l-cysteine deficiency and subsequent impairment of glutathione metabolism, as well as higher plasma homocysteine concentrations.13, 14, 15, 16, 17 Besides its role in the conversion of l-cystathionine into l-cysteine, studies have also shown that CSE can utilize l-cysteine as a substrate for producing H2S via an α,β-elimination reaction (Fig. 1).18, 19, 20 However, to date, no reports have clearly demonstrated the residues that affect CSE-mediated H2S production. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
Kidney, Liver, Vascular Cell |
4.0
CTH
- 
- 