Page last updated: 2024-08-07 10:17:05

Cystathionine gamma-lyase

A cystathionine gamma-lyase that is encoded in the genome of human. [PRO:DNx, UniProtKB:P32929]

Synonyms

EC 4.4.1.1;
Cysteine-protein sulfhydrase;
Gamma-cystathionase

Research

Bioassay Publications (4)

TimeframeStudies on this Protein(%)All Drugs %
pre-19900 (0.00)18.7374
1990's0 (0.00)18.2507
2000's0 (0.00)29.6817
2010's4 (100.00)24.3611
2020's0 (0.00)2.80

Compounds (15)

Drugs with Inhibition Measurements

DrugTaxonomyMeasurementAverage (mM)Bioassay(s)Publication(s)
aminooxyacetic acidHomo sapiens (human)IC502.285022
salicylic acidHomo sapiens (human)IC50200.000011
aurintricarboxylic acidHomo sapiens (human)IC5094.50001010
aurintricarboxylic acidHomo sapiens (human)Ki0.600011
mesalamineHomo sapiens (human)IC50200.000011
penicillamineHomo sapiens (human)IC50270.000011
nitroxolineHomo sapiens (human)IC508.233333
olsalazineHomo sapiens (human)IC50200.000011
methyldopaHomo sapiens (human)IC503,000.000011
6-amino-7-chloro-5,8-dioxoquinolineHomo sapiens (human)IC5050.000011
kalafunginHomo sapiens (human)IC5050.000011
nsc228155Homo sapiens (human)IC5050.000011
agathisflavoneHomo sapiens (human)IC50400.000011
cupressuflavoneHomo sapiens (human)IC50400.000011
podocarpusflavone aHomo sapiens (human)IC50400.000011
aminoethoxyvinylglycineHomo sapiens (human)IC501.100011

Drugs with Activation Measurements

DrugTaxonomyMeasurementAverage (mM)Bioassay(s)Publication(s)
aurintricarboxylic acidHomo sapiens (human)Kd3.400011

Drugs with Other Measurements

DrugTaxonomyMeasurementAverage (mM)Bioassay(s)Publication(s)
aurintricarboxylic acidHomo sapiens (human)alphaKi4.200011

Enables

This protein enables 9 target(s):

TargetCategoryDefinition
cystathionine gamma-lyase activitymolecular functionCatalysis of the reaction: L-cystathionine + H2O = 2-oxobutanoate + L-cysteine + NH4+. [RHEA:14005]
protein bindingmolecular functionBinding to a protein. [GOC:go_curators]
calmodulin bindingmolecular functionBinding to calmodulin, a calcium-binding protein with many roles, both in the calcium-bound and calcium-free states. [GOC:krc]
pyridoxal phosphate bindingmolecular functionBinding to pyridoxal 5' phosphate, 3-hydroxy-5-(hydroxymethyl)-2-methyl4-pyridine carboxaldehyde 5' phosphate, the biologically active form of vitamin B6. [GOC:mah, ISBN:0198506732]
identical protein bindingmolecular functionBinding to an identical protein or proteins. [GOC:jl]
L-cystine L-cysteine-lyase (deaminating)molecular functionCatalysis of the reaction: L-cystine + H2O = pyruvate + NH3 + thiocysteine. Thiocysteine is also known as cysteine persulfide. [GOC:jl, RHEA:24927]
homocysteine desulfhydrase activitymolecular functionCatalysis of the reaction: L-homocysteine + H2O = sulfide + NH3 + 2-oxobutanoate. [EC:4.4.1.2, MetaCyc:HOMOCYSTEINE-DESULFHYDRASE-RXN]
L-cysteine desulfhydrase activitymolecular functionCatalysis of the reaction: L-cysteine + H2O = ammonia + pyruvate + hydrogen sulfide + H+. [MetaCyc:LCYSDESULF-RXN, PMID:19955263]
selenocystathionine gamma-lyase activitymolecular functionCatalysis of the reaction: L-Selenocystathionine + H2O => L-Selenocysteine + NH3 + 2-Oxobutanoic acid. [PMID:6456763]

Located In

This protein is located in 2 target(s):

TargetCategoryDefinition
cytosolcellular componentThe part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes. [GOC:hjd, GOC:jl]
extracellular exosomecellular componentA vesicle that is released into the extracellular region by fusion of the limiting endosomal membrane of a multivesicular body with the plasma membrane. Extracellular exosomes, also simply called exosomes, have a diameter of about 40-100 nm. [GOC:BHF, GOC:mah, GOC:vesicles, PMID:15908444, PMID:17641064, PMID:19442504, PMID:19498381, PMID:22418571, PMID:24009894]

Active In

This protein is active in 1 target(s):

TargetCategoryDefinition
cytoplasmcellular componentThe contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. [ISBN:0198547684]

Involved In

This protein is involved in 14 target(s):

TargetCategoryDefinition
cysteine metabolic processbiological processThe chemical reactions and pathways involving cysteine, 2-amino-3-mercaptopropanoic acid. [GOC:go_curators]
lipid metabolic processbiological processThe chemical reactions and pathways involving lipids, compounds soluble in an organic solvent but not, or sparingly, in an aqueous solvent. Includes fatty acids; neutral fats, other fatty-acid esters, and soaps; long-chain (fatty) alcohols and waxes; sphingoids and other long-chain bases; glycolipids, phospholipids and sphingolipids; and carotenes, polyprenols, sterols, terpenes and other isoprenoids. [GOC:ma]
protein-pyridoxal-5-phosphate linkage via peptidyl-N6-pyridoxal phosphate-L-lysinebiological processThe modification of peptidyl-lysine to form N6-pyridoxal phosphate-L-lysine. [RESID:AA0119]
cysteine biosynthetic process via cystathioninebiological processThe chemical reactions and pathways resulting in the formation of cysteine, via the intermediate cystathionine. [GOC:go_curators]
cysteine biosynthetic processbiological processThe chemical reactions and pathways resulting in the formation of cysteine, 2-amino-3-mercaptopropanoic acid. [GOC:go_curators]
transsulfurationbiological processThe interconversion of homocysteine and cysteine via cystathionine. In contrast with enteric bacteria and mammals, Saccharomyces cerevisiae has two transsulfuration pathways employing two separate sets of enzymes. [MetaCyc:PWY-801]
endoplasmic reticulum unfolded protein responsebiological processThe series of molecular signals generated as a consequence of the presence of unfolded proteins in the endoplasmic reticulum (ER) or other ER-related stress; results in changes in the regulation of transcription and translation. [GOC:mah, PMID:12042763]
positive regulation of canonical NF-kappaB signal transductionbiological processAny process that activates or increases the frequency, rate or extent of a canonical NF-kappaB signaling cascade. [GOC:jl]
protein sulfhydrationbiological processThe modification of a protein amino acid by the addition of sulfur. [GOC:jl, GOC:jsg, PMID:19903941, PMID:22169477, PMID:8161529]
protein homotetramerizationbiological processThe formation of a protein homotetramer, a macromolecular structure consisting of four noncovalently associated identical subunits. [GOC:go_curators]
hydrogen sulfide biosynthetic processbiological processThe chemical reactions and pathways resulting in the formation of hydrogen sulfide, H2S. [GOC:mah]
positive regulation of aortic smooth muscle cell differentiationbiological processAny process that activates or increases the frequency, rate or extent of aortic smooth muscle cell differentiation. [GO_REF:0000058, GOC:BHF, GOC:BHF_miRNA, GOC:rph, GOC:TermGenie, PMID:22034194]
cellular response to leukemia inhibitory factorbiological processAny process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a leukemia inhibitory factor stimulus. [PMID:12801913]
negative regulation of apoptotic signaling pathwaybiological processAny process that stops, prevents or reduces the frequency, rate or extent of apoptotic signaling pathway. [GOC:mtg_apoptosis]