What is the fate of sulfur in cysteine when it participates in gluconeogenesis?What happens to the NADH produced by lactate oxidation?Ionization of amino acidsHow do thiol groups act as reducing agents?Why does adding a charged group to an organic molecule decrease its stability?Do any efforts to construct artificial biochemistries exist and what compounds are they based on?Why is fermentation of cellulose to produce biofuel and nutrients so difficult?Extracting metallic magnesium from cholorphyllDoes oxidation of fatty acids through the process of ketosis versus direct beta oxidation change ATP production?What is the precise definition of Ramachandran angles?Is hydrolysis of polypeptides and polysaccharides “anabolic” or “catabolic”
Should I take out a personal loan to pay off credit card debt?
Why do proponents of guns oppose gun competency tests?
Should I self-publish my novella on Amazon or try my luck getting publishers?
Making pause in a diagram
Can a Hogwarts student refuse the Sorting Hat's decision?
Does this put me at risk for identity theft?
Why is Chromosome 1 called Chromosome 1?
Will a paper be retracted if a flaw in released software code invalidates its central idea?
What word best describes someone who likes to do everything on his own?
Probably terminated or laid off soon; confront or not?
12V lead acid charger with LM317 not charging
Why do private jets such as Gulfstream fly higher than other civilian jets?
Best way to explain to my boss that I cannot attend a team summit because it is on Rosh Hashana or any other Jewish Holiday
Generate a random point outside a given rectangle within a map
How to check a file was encrypted (really & correctly)
Is there such thing as a "3-dimensional surface?"
Can chords be inferred from melody alone?
monolingual dictionary
"In charge of" vs "Responsible for"
What is a Casino Word™?
Is it a bad idea to offer variants of a final exam based on the type of allowed calculators?
Count number of occurences of particular numbers in list
How to switch an 80286 from protected to real mode?
Premier League simulation
What is the fate of sulfur in cysteine when it participates in gluconeogenesis?
What happens to the NADH produced by lactate oxidation?Ionization of amino acidsHow do thiol groups act as reducing agents?Why does adding a charged group to an organic molecule decrease its stability?Do any efforts to construct artificial biochemistries exist and what compounds are they based on?Why is fermentation of cellulose to produce biofuel and nutrients so difficult?Extracting metallic magnesium from cholorphyllDoes oxidation of fatty acids through the process of ketosis versus direct beta oxidation change ATP production?What is the precise definition of Ramachandran angles?Is hydrolysis of polypeptides and polysaccharides “anabolic” or “catabolic”
.everyoneloves__top-leaderboard:empty,.everyoneloves__mid-leaderboard:empty,.everyoneloves__bot-mid-leaderboard:empty margin-bottom:0;
$begingroup$
Amino acids can be broken down to yield pyruvate, which in turn can be used to construct glucose molecule in the process of gluconeogenesis. What happens to the sulfur atom in the amino acid cysteine when it is processed into pyruvate?
Image source: NCBI Bookshelf
biochemistry
edited Jul 27 at 20:07
andselisk♦
21.9k8 gold badges77 silver badges147 bronze badges
asked Jul 27 at 19:54
Joseph HirschJoseph Hirsch
7534 silver badges15 bronze badges
$endgroup$
add a comment |
$begingroup$
Amino acids can be broken down to yield pyruvate, which in turn can be used to construct glucose molecule in the process of gluconeogenesis. What happens to the sulfur atom in the amino acid cysteine when it is processed into pyruvate?
Image source: NCBI Bookshelf
biochemistry
edited Jul 27 at 20:07
andselisk♦
21.9k8 gold badges77 silver badges147 bronze badges
asked Jul 27 at 19:54
Joseph HirschJoseph Hirsch
7534 silver badges15 bronze badges
$endgroup$
add a comment |
$begingroup$
Amino acids can be broken down to yield pyruvate, which in turn can be used to construct glucose molecule in the process of gluconeogenesis. What happens to the sulfur atom in the amino acid cysteine when it is processed into pyruvate?
Image source: NCBI Bookshelf
biochemistry
edited Jul 27 at 20:07
andselisk♦
21.9k8 gold badges77 silver badges147 bronze badges
asked Jul 27 at 19:54
Joseph HirschJoseph Hirsch
7534 silver badges15 bronze badges
$endgroup$
Amino acids can be broken down to yield pyruvate, which in turn can be used to construct glucose molecule in the process of gluconeogenesis. What happens to the sulfur atom in the amino acid cysteine when it is processed into pyruvate?
Image source: NCBI Bookshelf
biochemistry
biochemistry
edited Jul 27 at 20:07
andselisk♦
21.9k8 gold badges77 silver badges147 bronze badges
asked Jul 27 at 19:54
Joseph HirschJoseph Hirsch
7534 silver badges15 bronze badges
edited Jul 27 at 20:07
andselisk♦
21.9k8 gold badges77 silver badges147 bronze badges
asked Jul 27 at 19:54
Joseph HirschJoseph Hirsch
7534 silver badges15 bronze badges
edited Jul 27 at 20:07
andselisk♦
21.9k8 gold badges77 silver badges147 bronze badges
edited Jul 27 at 20:07
andselisk♦
21.9k8 gold badges77 silver badges147 bronze badges
edited Jul 27 at 20:07
andselisk♦
21.9k8 gold badges77 silver badges147 bronze badges
21.9k8 gold badges77 silver badges147 bronze badges
asked Jul 27 at 19:54
Joseph HirschJoseph Hirsch
7534 silver badges15 bronze badges
asked Jul 27 at 19:54
Joseph HirschJoseph Hirsch
7534 silver badges15 bronze badges
asked Jul 27 at 19:54
Joseph HirschJoseph Hirsch
7534 silver badges15 bronze badges
7534 silver badges15 bronze badges
add a comment |
add a comment |
2 Answers
2
active
oldest
votes
$begingroup$
Cysteine is a dispensable amino acid required for synthesis of protein and non-protein compounds. These non-protein compounds include pyruate (hence acetyl coenzyme A), taurine, sulfate, and glutatione (GSH). The fate of the cycteine is hence sketched in following diagram (Ref.1):
As evidence from the diagram, the sulfur atom in cysteine has been converted to sulfate ion ($ceSO4^2-$) through $ceHS-$ ion. This fact has been previously proved experimentally (Ref.2). Accordingly, the first major step in cysteine catabolism in mammalian tissues is the oxidation of cysteine to cysteine sulfinic acid catalyzes by cysteine dioxygenase (CDO). The reaction mechanism of this non-heme iron dioxygenase has been recently reviewed (Ref.3).
References:
- G. Courtney-Martin, P. B. Pencharz, “Chapter 19: Sulfur Amino Acids Metabolism From Protein Synthesis to Glutathione,“ In The Molecular Nutrition of Amino Acids and Proteins; Dominique Dardevet, Ed.; Academic Press, Elsevier Inc.: London, United Kingdom, 2016, pp. 265-286 (https://doi.org/10.1016/C2014-0-02227-7).
- Catherine L. Weinstein, Rudy H. Haschemeyer, Owen W. Griffith, “In vivo studies of cysteine metabolism. Use of D-cysteinesulfinate, a novel cysteinesulfinate decarboxylase inhibitor, to probe taurine and pyruvate synthesis,” The Journal of Biological Chemistry 1988, 263(32), 16568-16579 (http://www.jbc.org/content/263/32/16568.full.pdf+html).
- Crisjoe A. Josepha, Michael J. Maroney, “Cysteine dioxygenase: structure and mechanism,” Chem. Commun. 2007, (32), 3338-3349 (DOI: 10.1039/B702158E).
answered Jul 28 at 2:27
Mathew MahindaratneMathew Mahindaratne
10.9k1 gold badge12 silver badges38 bronze badges
$endgroup$
add a comment |
$begingroup$
According to https://www.uniprot.org/uniprot/P25325, 3-mercaptopyruvate sulfurtransferase is also involved in the catabolism of cysteine:
Transfer of a sulfur ion to cyanide or to other thiol compounds. Also has weak rhodanese activity. Detoxifies cyanide and is required for thiosulfate biosynthesis. Acts as an antioxidant. In combination with cysteine aminotransferase (CAT), contributes to the catabolism of cysteine and is an important producer of hydrogen sulfide in the brain, retina and vascular endothelial cells. Hydrogen sulfide H2S is an important synaptic modulator, signaling molecule, smooth muscle contractor and neuroprotectant. Its production by the 3MST/CAT pathway is regulated by calcium ions.
answered Jul 28 at 3:18
Karsten TheisKarsten Theis
9,17812 silver badges54 bronze badges
$endgroup$
add a comment |
Your Answer
StackExchange.ready(function()
var channelOptions =
tags: "".split(" "),
id: "431"
;
initTagRenderer("".split(" "), "".split(" "), channelOptions);
StackExchange.using("externalEditor", function()
// Have to fire editor after snippets, if snippets enabled
if (StackExchange.settings.snippets.snippetsEnabled)
StackExchange.using("snippets", function()
createEditor();
);
else
createEditor();
);
function createEditor()
StackExchange.prepareEditor(
heartbeatType: 'answer',
autoActivateHeartbeat: false,
convertImagesToLinks: false,
noModals: true,
showLowRepImageUploadWarning: true,
reputationToPostImages: null,
bindNavPrevention: true,
postfix: "",
imageUploader:
brandingHtml: "Powered by u003ca class="icon-imgur-white" href="https://imgur.com/"u003eu003c/au003e",
contentPolicyHtml: "User contributions licensed under u003ca href="https://creativecommons.org/licenses/by-sa/3.0/"u003ecc by-sa 3.0 with attribution requiredu003c/au003e u003ca href="https://stackoverflow.com/legal/content-policy"u003e(content policy)u003c/au003e",
allowUrls: true
,
onDemand: true,
discardSelector: ".discard-answer"
,immediatelyShowMarkdownHelp:true
);
);
Sign up or log in
StackExchange.ready(function ()
StackExchange.helpers.onClickDraftSave('#login-link');
);
Sign up using Google
Sign up using Facebook
Sign up using Email and Password
Post as a guest
Required, but never shown
StackExchange.ready(
function ()
StackExchange.openid.initPostLogin('.new-post-login', 'https%3a%2f%2fchemistry.stackexchange.com%2fquestions%2f118572%2fwhat-is-the-fate-of-sulfur-in-cysteine-when-it-participates-in-gluconeogenesis%23new-answer', 'question_page');
);
Post as a guest
Required, but never shown
2 Answers
2
active
oldest
votes
2 Answers
2
active
oldest
votes
active
oldest
votes
active
oldest
votes
$begingroup$
Cysteine is a dispensable amino acid required for synthesis of protein and non-protein compounds. These non-protein compounds include pyruate (hence acetyl coenzyme A), taurine, sulfate, and glutatione (GSH). The fate of the cycteine is hence sketched in following diagram (Ref.1):
As evidence from the diagram, the sulfur atom in cysteine has been converted to sulfate ion ($ceSO4^2-$) through $ceHS-$ ion. This fact has been previously proved experimentally (Ref.2). Accordingly, the first major step in cysteine catabolism in mammalian tissues is the oxidation of cysteine to cysteine sulfinic acid catalyzes by cysteine dioxygenase (CDO). The reaction mechanism of this non-heme iron dioxygenase has been recently reviewed (Ref.3).
References:
- G. Courtney-Martin, P. B. Pencharz, “Chapter 19: Sulfur Amino Acids Metabolism From Protein Synthesis to Glutathione,“ In The Molecular Nutrition of Amino Acids and Proteins; Dominique Dardevet, Ed.; Academic Press, Elsevier Inc.: London, United Kingdom, 2016, pp. 265-286 (https://doi.org/10.1016/C2014-0-02227-7).
- Catherine L. Weinstein, Rudy H. Haschemeyer, Owen W. Griffith, “In vivo studies of cysteine metabolism. Use of D-cysteinesulfinate, a novel cysteinesulfinate decarboxylase inhibitor, to probe taurine and pyruvate synthesis,” The Journal of Biological Chemistry 1988, 263(32), 16568-16579 (http://www.jbc.org/content/263/32/16568.full.pdf+html).
- Crisjoe A. Josepha, Michael J. Maroney, “Cysteine dioxygenase: structure and mechanism,” Chem. Commun. 2007, (32), 3338-3349 (DOI: 10.1039/B702158E).
answered Jul 28 at 2:27
Mathew MahindaratneMathew Mahindaratne
10.9k1 gold badge12 silver badges38 bronze badges
$endgroup$
add a comment |
$begingroup$
Cysteine is a dispensable amino acid required for synthesis of protein and non-protein compounds. These non-protein compounds include pyruate (hence acetyl coenzyme A), taurine, sulfate, and glutatione (GSH). The fate of the cycteine is hence sketched in following diagram (Ref.1):
As evidence from the diagram, the sulfur atom in cysteine has been converted to sulfate ion ($ceSO4^2-$) through $ceHS-$ ion. This fact has been previously proved experimentally (Ref.2). Accordingly, the first major step in cysteine catabolism in mammalian tissues is the oxidation of cysteine to cysteine sulfinic acid catalyzes by cysteine dioxygenase (CDO). The reaction mechanism of this non-heme iron dioxygenase has been recently reviewed (Ref.3).
References:
- G. Courtney-Martin, P. B. Pencharz, “Chapter 19: Sulfur Amino Acids Metabolism From Protein Synthesis to Glutathione,“ In The Molecular Nutrition of Amino Acids and Proteins; Dominique Dardevet, Ed.; Academic Press, Elsevier Inc.: London, United Kingdom, 2016, pp. 265-286 (https://doi.org/10.1016/C2014-0-02227-7).
- Catherine L. Weinstein, Rudy H. Haschemeyer, Owen W. Griffith, “In vivo studies of cysteine metabolism. Use of D-cysteinesulfinate, a novel cysteinesulfinate decarboxylase inhibitor, to probe taurine and pyruvate synthesis,” The Journal of Biological Chemistry 1988, 263(32), 16568-16579 (http://www.jbc.org/content/263/32/16568.full.pdf+html).
- Crisjoe A. Josepha, Michael J. Maroney, “Cysteine dioxygenase: structure and mechanism,” Chem. Commun. 2007, (32), 3338-3349 (DOI: 10.1039/B702158E).
answered Jul 28 at 2:27
Mathew MahindaratneMathew Mahindaratne
10.9k1 gold badge12 silver badges38 bronze badges
$endgroup$
add a comment |
$begingroup$
Cysteine is a dispensable amino acid required for synthesis of protein and non-protein compounds. These non-protein compounds include pyruate (hence acetyl coenzyme A), taurine, sulfate, and glutatione (GSH). The fate of the cycteine is hence sketched in following diagram (Ref.1):
As evidence from the diagram, the sulfur atom in cysteine has been converted to sulfate ion ($ceSO4^2-$) through $ceHS-$ ion. This fact has been previously proved experimentally (Ref.2). Accordingly, the first major step in cysteine catabolism in mammalian tissues is the oxidation of cysteine to cysteine sulfinic acid catalyzes by cysteine dioxygenase (CDO). The reaction mechanism of this non-heme iron dioxygenase has been recently reviewed (Ref.3).
References:
- G. Courtney-Martin, P. B. Pencharz, “Chapter 19: Sulfur Amino Acids Metabolism From Protein Synthesis to Glutathione,“ In The Molecular Nutrition of Amino Acids and Proteins; Dominique Dardevet, Ed.; Academic Press, Elsevier Inc.: London, United Kingdom, 2016, pp. 265-286 (https://doi.org/10.1016/C2014-0-02227-7).
- Catherine L. Weinstein, Rudy H. Haschemeyer, Owen W. Griffith, “In vivo studies of cysteine metabolism. Use of D-cysteinesulfinate, a novel cysteinesulfinate decarboxylase inhibitor, to probe taurine and pyruvate synthesis,” The Journal of Biological Chemistry 1988, 263(32), 16568-16579 (http://www.jbc.org/content/263/32/16568.full.pdf+html).
- Crisjoe A. Josepha, Michael J. Maroney, “Cysteine dioxygenase: structure and mechanism,” Chem. Commun. 2007, (32), 3338-3349 (DOI: 10.1039/B702158E).
answered Jul 28 at 2:27
Mathew MahindaratneMathew Mahindaratne
10.9k1 gold badge12 silver badges38 bronze badges
$endgroup$
Cysteine is a dispensable amino acid required for synthesis of protein and non-protein compounds. These non-protein compounds include pyruate (hence acetyl coenzyme A), taurine, sulfate, and glutatione (GSH). The fate of the cycteine is hence sketched in following diagram (Ref.1):
As evidence from the diagram, the sulfur atom in cysteine has been converted to sulfate ion ($ceSO4^2-$) through $ceHS-$ ion. This fact has been previously proved experimentally (Ref.2). Accordingly, the first major step in cysteine catabolism in mammalian tissues is the oxidation of cysteine to cysteine sulfinic acid catalyzes by cysteine dioxygenase (CDO). The reaction mechanism of this non-heme iron dioxygenase has been recently reviewed (Ref.3).
References:
- G. Courtney-Martin, P. B. Pencharz, “Chapter 19: Sulfur Amino Acids Metabolism From Protein Synthesis to Glutathione,“ In The Molecular Nutrition of Amino Acids and Proteins; Dominique Dardevet, Ed.; Academic Press, Elsevier Inc.: London, United Kingdom, 2016, pp. 265-286 (https://doi.org/10.1016/C2014-0-02227-7).
- Catherine L. Weinstein, Rudy H. Haschemeyer, Owen W. Griffith, “In vivo studies of cysteine metabolism. Use of D-cysteinesulfinate, a novel cysteinesulfinate decarboxylase inhibitor, to probe taurine and pyruvate synthesis,” The Journal of Biological Chemistry 1988, 263(32), 16568-16579 (http://www.jbc.org/content/263/32/16568.full.pdf+html).
- Crisjoe A. Josepha, Michael J. Maroney, “Cysteine dioxygenase: structure and mechanism,” Chem. Commun. 2007, (32), 3338-3349 (DOI: 10.1039/B702158E).
answered Jul 28 at 2:27
Mathew MahindaratneMathew Mahindaratne
10.9k1 gold badge12 silver badges38 bronze badges
answered Jul 28 at 2:27
Mathew MahindaratneMathew Mahindaratne
10.9k1 gold badge12 silver badges38 bronze badges
answered Jul 28 at 2:27
Mathew MahindaratneMathew Mahindaratne
10.9k1 gold badge12 silver badges38 bronze badges
answered Jul 28 at 2:27
Mathew MahindaratneMathew Mahindaratne
10.9k1 gold badge12 silver badges38 bronze badges
10.9k1 gold badge12 silver badges38 bronze badges
add a comment |
add a comment |
$begingroup$
According to https://www.uniprot.org/uniprot/P25325, 3-mercaptopyruvate sulfurtransferase is also involved in the catabolism of cysteine:
Transfer of a sulfur ion to cyanide or to other thiol compounds. Also has weak rhodanese activity. Detoxifies cyanide and is required for thiosulfate biosynthesis. Acts as an antioxidant. In combination with cysteine aminotransferase (CAT), contributes to the catabolism of cysteine and is an important producer of hydrogen sulfide in the brain, retina and vascular endothelial cells. Hydrogen sulfide H2S is an important synaptic modulator, signaling molecule, smooth muscle contractor and neuroprotectant. Its production by the 3MST/CAT pathway is regulated by calcium ions.
answered Jul 28 at 3:18
Karsten TheisKarsten Theis
9,17812 silver badges54 bronze badges
$endgroup$
add a comment |
$begingroup$
According to https://www.uniprot.org/uniprot/P25325, 3-mercaptopyruvate sulfurtransferase is also involved in the catabolism of cysteine:
Transfer of a sulfur ion to cyanide or to other thiol compounds. Also has weak rhodanese activity. Detoxifies cyanide and is required for thiosulfate biosynthesis. Acts as an antioxidant. In combination with cysteine aminotransferase (CAT), contributes to the catabolism of cysteine and is an important producer of hydrogen sulfide in the brain, retina and vascular endothelial cells. Hydrogen sulfide H2S is an important synaptic modulator, signaling molecule, smooth muscle contractor and neuroprotectant. Its production by the 3MST/CAT pathway is regulated by calcium ions.
answered Jul 28 at 3:18
Karsten TheisKarsten Theis
9,17812 silver badges54 bronze badges
$endgroup$
add a comment |
$begingroup$
According to https://www.uniprot.org/uniprot/P25325, 3-mercaptopyruvate sulfurtransferase is also involved in the catabolism of cysteine:
Transfer of a sulfur ion to cyanide or to other thiol compounds. Also has weak rhodanese activity. Detoxifies cyanide and is required for thiosulfate biosynthesis. Acts as an antioxidant. In combination with cysteine aminotransferase (CAT), contributes to the catabolism of cysteine and is an important producer of hydrogen sulfide in the brain, retina and vascular endothelial cells. Hydrogen sulfide H2S is an important synaptic modulator, signaling molecule, smooth muscle contractor and neuroprotectant. Its production by the 3MST/CAT pathway is regulated by calcium ions.
answered Jul 28 at 3:18
Karsten TheisKarsten Theis
9,17812 silver badges54 bronze badges
$endgroup$
According to https://www.uniprot.org/uniprot/P25325, 3-mercaptopyruvate sulfurtransferase is also involved in the catabolism of cysteine:
Transfer of a sulfur ion to cyanide or to other thiol compounds. Also has weak rhodanese activity. Detoxifies cyanide and is required for thiosulfate biosynthesis. Acts as an antioxidant. In combination with cysteine aminotransferase (CAT), contributes to the catabolism of cysteine and is an important producer of hydrogen sulfide in the brain, retina and vascular endothelial cells. Hydrogen sulfide H2S is an important synaptic modulator, signaling molecule, smooth muscle contractor and neuroprotectant. Its production by the 3MST/CAT pathway is regulated by calcium ions.
answered Jul 28 at 3:18
Karsten TheisKarsten Theis
9,17812 silver badges54 bronze badges
answered Jul 28 at 3:18
Karsten TheisKarsten Theis
9,17812 silver badges54 bronze badges
answered Jul 28 at 3:18
Karsten TheisKarsten Theis
9,17812 silver badges54 bronze badges
answered Jul 28 at 3:18
Karsten TheisKarsten Theis
9,17812 silver badges54 bronze badges
9,17812 silver badges54 bronze badges
add a comment |
add a comment |
Thanks for contributing an answer to Chemistry Stack Exchange!
- Please be sure to answer the question. Provide details and share your research!
But avoid …
- Asking for help, clarification, or responding to other answers.
- Making statements based on opinion; back them up with references or personal experience.
Use MathJax to format equations. MathJax reference.
To learn more, see our tips on writing great answers.
Sign up or log in
StackExchange.ready(function ()
StackExchange.helpers.onClickDraftSave('#login-link');
);
Sign up using Google
Sign up using Facebook
Sign up using Email and Password
Post as a guest
Required, but never shown
StackExchange.ready(
function ()
StackExchange.openid.initPostLogin('.new-post-login', 'https%3a%2f%2fchemistry.stackexchange.com%2fquestions%2f118572%2fwhat-is-the-fate-of-sulfur-in-cysteine-when-it-participates-in-gluconeogenesis%23new-answer', 'question_page');
);
Post as a guest
Required, but never shown
Sign up or log in
StackExchange.ready(function ()
StackExchange.helpers.onClickDraftSave('#login-link');
);
Sign up using Google
Sign up using Facebook
Sign up using Email and Password
Post as a guest
Required, but never shown
Sign up or log in
StackExchange.ready(function ()
StackExchange.helpers.onClickDraftSave('#login-link');
);
Sign up using Google
Sign up using Facebook
Sign up using Email and Password
Post as a guest
Required, but never shown
Sign up or log in
StackExchange.ready(function ()
StackExchange.helpers.onClickDraftSave('#login-link');
);
Sign up using Google
Sign up using Facebook
Sign up using Email and Password
Sign up using Google
Sign up using Facebook
Sign up using Email and Password
Post as a guest
Required, but never shown
Required, but never shown
Required, but never shown
Required, but never shown
Required, but never shown
Required, but never shown
Required, but never shown
Required, but never shown
Required, but never shown
