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Literature summary for 4.4.1.4 extracted from
- Discovery and characterization of a novel lachrymatory factor synthase in Petiveria alliacea and its influence on alliinase-mediated formation of biologically active organosulfur compounds (2009), Plant Physiol., 151, 1294-1303.
Application
| Application | Comment | Organism |
|---|---|---|
| biotechnology | lachrymatory factor synthase and alliinase function in tandem, with the alliinase furnishing the sulfenic acid substrate on which the lachrymatory factor synthase acts. The lachrymatory factor synthase modulates the formation of biologically active thiosulfinates that are downstream of the alliinase in a manner dependent upon the relative concentrations of the lachrymatory factor synthase and the alliinase. These observations suggest that manipulation of lachrymatory factor synthase-to-alliinase ratios in plants displaying this system may provide a means by which to rationally modify organosulfur small molecule profiles to obtain desired flavor and/or odor signatures, or increase the presence of desirable biologically active small molecules | Petiveria alliacea |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| S-(2-hydroxyethyl)-L-cysteine sulfoxide | Petiveria alliacea | - |
? + pyruvate + NH3 | - |
? |  |
| S-benzyl-L-cysteine sulfoxide | Petiveria alliacea | - |
phenylmethanesulfenic acid + pyruvate + NH3 | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Petiveria alliacea | - |
- |
- |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| root | - |
Petiveria alliacea | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| S-(2-hydroxyethyl)-L-cysteine sulfoxide | - |
Petiveria alliacea | ? + pyruvate + NH3 | - |
? | |
| S-benzyl-L-cysteine sulfoxide | - |
Petiveria alliacea | phenylmethanesulfenic acid + pyruvate + NH3 | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| alliinase | - |
Petiveria alliacea |
pI Value
| Organism | Comment | pI Value Maximum | pI Value |
|---|---|---|---|
| Petiveria alliacea | chromatofocusing | - |
4.78 |
General Information
| General Information | Comment | Organism |
|---|---|---|
| metabolism | lachrymatory factor synthase and alliinase function in tandem, with the alliinase furnishing the sulfenic acid substrate on which the lachrymatory factor synthase acts. The lachrymatory factor synthase modulates the formation of biologically active thiosulfinates that are downstream of the alliinase in a manner dependent upon the relative concentrations of the lachrymatory factor synthase and the alliinase. These observations suggest that manipulation of lachrymatory factor synthase-to-alliinase ratios in plants displaying this system may provide a means by which to rationally modify organosulfur small molecule profiles to obtain desired flavor and/or odor signatures, or increase the presence of desirable biologically active small molecules | Petiveria alliacea |
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Release 2023.1 (January 2023)
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