Cysteine desulfurase: Difference between revisions

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cysteine desulfurase
cysteine desulfurase
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EC no.	2.8.1.7
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In enzymology, a cysteine desulfurase (EC 2.8.1.7) is an enzyme that catalyzes the chemical reaction

L-cysteine + [enzyme]-cysteine

\rightleftharpoons

L-alanine + [enzyme]-S-sulfanylcysteine

Thus, the two substrates of this enzyme are L-cysteine and [enzyme]-cysteine], whereas its two products are L-alanine and [enzyme]-S-sulfanylcysteine. One group of authors has given it the acronym hapE, for hydrogen sulfide, alanine, and pyruvate producing enzyme.^[1]

This enzyme belongs to the family of transferases, specifically the sulfurtransferases, which transfer sulfur-containing groups. The systematic name of this enzyme class is L-cysteine:[enzyme cysteine] sulfurtransferase. Other names in common use include IscS, NIFS, NifS, SufS, and cysteine desulfurylase.

Function

Bacteria contain cysteine desulfurases to form iron sulfur clusters in proteins.^[2] However recently it has been shown that the enzyme, which produces hydrogen sulfide from cysteine, is also a virulence factor, namely for M.pneumoniae, in that it causes both α-hemolysis and β-haemolysis of red blood cells.^[1]

In mammals, the enzyme participates in thiamine metabolism.

Structural studies

As of late 2007, only one structure had been solved for this class of enzymes, with the PDB accession code 1T3I.

References

^ ^a ^b Großhennig, Stephanie; Ischebeck, Till; Gibhardt, Johannes; Busse, Julia; Feussner, Ivo; Stülke, Jörg (April 2016). "Hydrogen sulfide is a novel potential virulence factor of M ycoplasma pneumoniae : characterization of the unusual cysteine desulfurase/desulfhydrase HapE". Molecular Microbiology. 100 (1): 42–54. doi:10.1111/mmi.13300. ISSN 0950-382X. PMID 26711628.
^ Mihara H, Esaki N (2002). "Bacterial cysteine desulfurases: their function and mechanisms". Appl. Microbiol. Biotechnol. 60 (1–2): 12–23. doi:10.1007/s00253-002-1107-4. PMID 12382038. S2CID 23172939.

Zheng L, White RH, Cash VL, Jack RF, Dean DR (1993). "Cysteine desulfurase activity indicates a role for NIFS in metallocluster biosynthesis". Proc. Natl. Acad. Sci. U.S.A. 90 (7): 2754–8. Bibcode:1993PNAS...90.2754Z. doi:10.1073/pnas.90.7.2754. PMC 46174. PMID 8464885.
Frazzon J, Dean DR (2003). "Formation of iron-sulfur clusters in bacteria: an emerging field in bioinorganic chemistry". Curr. Opin. Chem. Biol. 7 (2): 166–73. doi:10.1016/S1367-5931(03)00021-8. PMID 12714048.

This EC 2.8 enzyme-related article is a stub. You can help Wikipedia by expanding it.

[Großhennig-1] Großhennig, Stephanie; Ischebeck, Till; Gibhardt, Johannes; Busse, Julia; Feussner, Ivo; Stülke, Jörg (April 2016). "Hydrogen sulfide is a novel potential virulence factor of M ycoplasma pneumoniae : characterization of the unusual cysteine desulfurase/desulfhydrase HapE". Molecular Microbiology. 100 (1): 42–54. doi:10.1111/mmi.13300. ISSN 0950-382X. PMID 26711628.

[2] Mihara H, Esaki N (2002). "Bacterial cysteine desulfurases: their function and mechanisms". Appl. Microbiol. Biotechnol. 60 (1–2): 12–23. doi:10.1007/s00253-002-1107-4. PMID 12382038. S2CID 23172939.

[1]

[2]

@@ Line 1: / Line 1: @@
+{{Short description|Class of enzymes}}
-{{enzyme
+{{infobox enzyme
-| Name = cysteine desulfurase
+| Name       = cysteine desulfurase
-| EC_number = 2.8.1.7
-| CAS_number =
+| EC_number  = 2.8.1.7
+| CAS_number =
-| IUBMB_EC_number = 2/8/1/7
-| GO_code = 0031071
+| GO_code    = 0031071
-| image =
+| image      =
-| width =
+| width      =
-| caption =
+| caption    =
 }}
 In [[enzymology]], a '''cysteine desulfurase''' ({{EC number|2.8.1.7}}) is an [[enzyme]] that [[catalysis|catalyzes]] the [[chemical reaction]]
@@ Line 13: / Line 13: @@
 :L-cysteine + [enzyme]-cysteine <math>\rightleftharpoons</math> L-alanine + [enzyme]-S-sulfanylcysteine
-Thus, the two [[substrate (biochemistry)|substrates]] of this enzyme are [[L-cysteine]] and [[[enzyme]-cysteine]], whereas its two [[product (chemistry)|products]] are [[L-alanine]] and [[[enzyme]-S-sulfanylcysteine]].
+Thus, the two [[substrate (biochemistry)|substrates]] of this enzyme are [[L-cysteine]] and [enzyme]-cysteine], whereas its two [[product (chemistry)|products]] are [[L-alanine]] and [enzyme]-S-sulfanylcysteine. One group of authors has given it the acronym '''hapE''', for hydrogen sulfide, alanine, and pyruvate producing enzyme.<ref name="Großhennig">{{Cite journal |last1=Großhennig |first1=Stephanie |last2=Ischebeck |first2=Till |last3=Gibhardt |first3=Johannes |last4=Busse |first4=Julia |last5=Feussner |first5=Ivo |last6=Stülke |first6=Jörg |date=April 2016 |title=Hydrogen sulfide is a novel potential virulence factor of M ycoplasma pneumoniae : characterization of the unusual cysteine desulfurase/desulfhydrase HapE |url=https://onlinelibrary.wiley.com/doi/10.1111/mmi.13300 |journal=Molecular Microbiology |language=en |volume=100 |issue=1 |pages=42–54 |doi=10.1111/mmi.13300 |pmid=26711628 |issn=0950-382X}}</ref>
-This enzyme belongs to the family of [[transferase]]s, specifically the sulfurtransferases, which transfer sulfur-containing groups.  The systematic name of this enzyme class is '''L-cysteine:[enzyme cysteine] sulfurtransferase'''. Other names in common use include '''IscS''', '''NIFS''', '''NifS''', '''SufS''', and '''cysteine desulfurylase'''.  This enzyme participates in [[thiamine metabolism]].
+This enzyme belongs to the family of [[transferase]]s, specifically the [[sulfurtransferase]]s, which transfer sulfur-containing groups.  The [[List of enzymes|systematic name]] of this enzyme class is L-cysteine:[enzyme cysteine] sulfurtransferase. Other names in common use include '''IscS''', '''NIFS''', '''NifS''', '''SufS''', and '''cysteine desulfurylase'''.
+==Function==
+Bacteria contain cysteine desulfurases to form [[iron sulfur cluster]]s in proteins.<ref>{{cite journal | vauthors = Mihara H, Esaki N | date = 2002 | title = Bacterial cysteine desulfurases: their function and mechanisms | journal = Appl. Microbiol. Biotechnol.  | volume = 60 | pages = 12&ndash;23  | pmid = 12382038 | doi = 10.1007/s00253-002-1107-4 | issue = 1–2 | s2cid = 23172939 }}</ref>
+However recently it has been shown that the enzyme, which produces [[hydrogen sulfide]] from cysteine, is also a [[virulence factor]], namely for [[M.pneumoniae]], in that it causes both [[α-hemolysis]] and [[β-haemolysis]] of red blood cells.<ref name="Großhennig"/>
+In mammals, the enzyme participates in [[thiamine metabolism]].
 ==Structural studies==
-As of late 2007, only one [[tertiary structure|structure]] has been solved for this class of enzymes, with the [[Protein Data Bank|PDB]] accession code {{PDB link|1T3I}}.
+As of late 2007, only one [[tertiary structure|structure]] had been solved for this class of enzymes, with the [[Protein Data Bank|PDB]] accession code {{PDB link|1T3I}}.
 ==References==
 {{reflist|1}}
-* {{cite journal | author = Zheng L, White RH, Cash VL, Jack RF, Dean DR | date = 1993 | title = Cysteine desulfurase activity indicates a role for NIFS in metallocluster biosynthesis | journal = Proc. Natl. Acad. Sci. U.S.A.  | volume = 90 | pages = 2754&ndash;8  | pmid = 8464885 | doi = 10.1073/pnas.90.7.2754 | issue = 7 | pmc = 46174 }}
+* {{cite journal | vauthors = Zheng L, White RH, Cash VL, Jack RF, Dean DR | date = 1993 | title = Cysteine desulfurase activity indicates a role for NIFS in metallocluster biosynthesis | journal = Proc. Natl. Acad. Sci. U.S.A.  | volume = 90 | pages = 2754&ndash;8  | pmid = 8464885 | doi = 10.1073/pnas.90.7.2754 | issue = 7 | pmc = 46174 | bibcode = 1993PNAS...90.2754Z | doi-access = free }}
+*
-* {{cite journal | author = Mihara H, Esaki N | date = 2002 | title = Bacterial cysteine desulfurases: their function and mechanisms | journal = Appl. Microbiol. Biotechnol.  | volume = 60 | pages = 12&ndash;23  | pmid = 12382038 | doi = 10.1007/s00253-002-1107-4 | issue = 1-2 }}
-* {{cite journal | author = Frazzon J, Dean DR | date = 2003 | title = Formation of iron-sulfur clusters in bacteria: an emerging field in bioinorganic chemistry | journal = Curr. Opin. Chem. Biol.  | volume = 7 | pages = 166&ndash;73  | pmid = 12714048 | doi = 10.1016/S1367-5931(03)00021-8 | issue = 2 }}
+* {{cite journal | vauthors = Frazzon J, Dean DR | date = 2003 | title = Formation of iron-sulfur clusters in bacteria: an emerging field in bioinorganic chemistry | journal = Curr. Opin. Chem. Biol.  | volume = 7 | pages = 166&ndash;73  | pmid = 12714048 | doi = 10.1016/S1367-5931(03)00021-8 | issue = 2 }}
 {{Sulfur-containing group transferases}}
 {{Enzymes}}
-{{Portal bar|Molecular and Cellular Biology|border=no}}
+{{Portal bar|Biology|border=no}}
-{{transferase-stub}}
 [[Category:EC 2.8.1]]
 [[Category:Enzymes of known structure]]
+{{2.8-enzyme-stub}}

v t e Transferases: sulfur-containing group (EC 2.8)
2.8.1: Sulfurtransferases	Thiosulfate sulfurtransferase Rhodanese 3-mercaptopyruvate sulfurtransferase thiosulfate—thiol sulfurtransferase tRNA sulfurtransferase thiosulfate—dithiol sulfurtransferase biotin synthase cysteine desulfurase lipoyl synthase molybdenum cofactor sulfurtransferase thiazole synthase molybdopterin synthase sulfurtransferase molybdopterin synthase tRNA-uridine 2-sulfurtransferase () tRNA-5-taurinomethyluridine 2-sulfurtransferase () tRNA-5-methyluridine⁵⁴ 2-sulfurtransferase () L-aspartate semialdehyde sulfurtransferase ()
2.8.2: Sulfotransferases	aryl sulfotransferase amine sulfotransferase estrone sulfotransferase chondroitin 4-sulfotransferase choline sulfotransferase UDP-N-acetylgalactosamine-4-sulfate sulfotransferase heparan sulfate-glucosamine N-sulfotransferase tyrosine-ester sulfotransferase Renilla-luciferin sulfotransferase galactosylceramide sulfotransferase psychosine sulfotransferase bile salt sulfotransferase steroid sulfotransferase thiol sulfotransferase chondroitin 6-sulfotransferase cortisol sulfotransferase triglucosylalkylacylglycerol sulfotransferase protein-tyrosine sulfotransferase keratan sulfotransferase aryl-sulfate sulfotransferase (heparan sulfate)-glucosamine 3-sulfotransferase 1 desulfoglucosinolate sulfotransferase flavonol 3-sulfotransferase quercetin-3-sulfate 3′-sulfotransferase quercetin-3-sulfate 4′-sulfotransferase quercetin-3,3′-bissulfate 7-sulfotransferase (heparan sulfate)-glucosamine 3-sulfotransferase 2 (heparan sulfate)-glucosamine 3-sulfotransferase 3 petromyzonol sulfotransferase scymnol sulfotransferase N-acetylgalactosamine 4-sulfate 6-O-sulfotransferase glycochenodeoxycholate sulfotransferase dermatan 4-sulfotransferase desulfo-A47934 sulfotransferase () trehalose 2-sulfotransferase () aliphatic desulfoglucosinolate sulfotransferase () hydroxyjasmonate sulfotransferase () ω-hydroxy-β-dihydromenaquinone-9 sulfotransferase (*) Alcohol sulfotransferase Tyrosylprotein sulfotransferase
2.8.3: CoA-transferases	Propionate CoA-transferase oxalate CoA-transferase malonate CoA-transferase 3-oxoacid CoA-transferase 3-oxoadipate CoA-transferase succinyl-CoA—Dcitramalate CoA-transferase acetate CoA-transferase butyrate—acetoacetate CoA-transferase citrate CoA-transferase citramalate CoA-transferase glutaconate CoA-transferase succinate—hydroxymethylglutarate CoA-transferase 5-hydroxypentanoate CoA-transferase succinyl-CoA:(R)-benzylsuccinate CoA-transferase formyl-CoA transferase cinnamoyl-CoA:phenyllactate CoA-transferase succinyl-CoA:acetate CoA-transferase () CoA:oxalate CoA-transferase () succinyl-CoA—D-citramalate CoA-transferase () L-carnitine CoA-transferase () succinyl-CoA—L-malate CoA-transferase () caffeate CoA-transferase () (R)-2-hydroxy-4-methylpentanoate CoA-transferase () bile acid CoA-transferase () succinyl-CoA:mesaconate CoA transferase (*)
2.8.4: Alkylthio	2.8.4: Coenzyme-B sulfoethylthiotransferase arsenate-mycothiol transferase tRNA-2-methylthio-N⁶-dimethylallyladenosine synthase () [ribosomal protein S12] (aspartate⁸⁹-C³)-methylthiotransferase () tRNA (N⁶-L-threonylcarbamoyladenosine³⁷-C²)-methylthiotransferase (*)
2.8.5:	2.8.5: S-sulfo-L-cysteine synthase (3-phospho-L-serine-dependent) () L-cysteine S-thiosulfotransferase ()

v t e Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Diffusion-limited enzyme Cofactor Enzyme catalysis
Regulation	Allosteric regulation Cooperativity Enzyme inhibitor Enzyme activator
Classification	EC number Enzyme superfamily Enzyme family List of enzymes
Kinetics	Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics
Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list) EC7 Translocases (list)