Difference between revisions of "Part:BBa K1998010"
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===Overview===
 
===Overview===
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This part is composed of the HydG gene. All organisms with [Fe] hydrogenase and sequenced genomes contain homologues of HydE, HydF, and HydG. Within several prokaryotic genomes HydE, HydF, and HydG are found in putative operons with [Fe] hydrogenase structural genes.
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This part is composed of the <i>hydG</i> gene. All organisms with [Fe] hydrogenase and sequenced genomes contain homologues of <i>hydE, hydF</i>, and <i>hydG</i>. Within several prokaryotic genomes <i>hydE, hydF</i>, and <i>hydG</i> are found in putative operons with [Fe] hydrogenase structural genes.
 
<br><br>
 
<br><br>
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<html><center><img src="https://static.igem.org/mediawiki/2016/8/81/T--Macquarie_Australia--HydrogenProduction.png" alt="HydrogenProduction" height="50%"width="75%"></center></html>
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<html><center><img src="https://static.igem.org/mediawiki/parts/b/b5/HydrogenPathwayUpdated2016.jpeg" alt="HydrogenProduction" height="50%"width="75%"></center></html>
  
 
===Biology & Literature===
 
===Biology & Literature===
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HydG is a radical S-adenosyl methionine (SAM) enzyme which catalyzes formation of a CO- and CN−-bound iron precursor to the H cluster, the cofactor on which [FeFe] hydrogenases are dependent on [1]. HydG breaks up the substrate tyrosine to yield both CO- and CN—ligands which act as precorsors during H-cluster assembly. It has been suggested that Hyd G cleaves the Cα–Cβ bond of tyrosine and p-cresol and dehydroglycine are formed as by-products [2]. Hyd E and Hyd F are maturases also required for the assembly of an active hydrogenase [3]. The binding site in HydG can accommodate either a [5Fe-5S] or a [4Fe-5S] cluster [4].
+
<i>hydG</i> is a radical S-adenosyl methionine (SAM) enzyme which catalyzes formation of a CO- and CN−-bound iron precursor to the H cluster, the cofactor on which [FeFe] hydrogenases are dependent on [1]. <i>hydG</i> breaks up the substrate tyrosine to yield both CO- and CN—ligands which act as precorsors during H-cluster assembly. It has been suggested that <i>hydG</i> cleaves the Cα–Cβ bond of tyrosine and p-cresol and dehydroglycine are formed as by-products [2]. <i>hydE</i> and <i>hydF</i> are maturases also required for the assembly of an active hydrogenase [3]. The binding site in <i>hydG</i> can accommodate either a [5Fe-5S] or a [4Fe-5S] cluster [4].
  
 
===Protein information===
 
===Protein information===
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HydG<br>
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<i>hydG</i><br>
 
Mass: 63.74kDa<br>
 
Mass: 63.74kDa<br>
 
Sequence: <br>
 
Sequence: <br>
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===References===
 
===References===
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[1] Dinis P, Suess D, Fox S, Harmer J, Driesener R, De La Paz L et al. X-ray crystallographic and EPR spectroscopic analysis of HydG, a maturase in [FeFe]-hydrogenase H-cluster assembly. Proceedings of the National Academy of Sciences. 2015;112(5):1362-1367.
+
[1] Dinis P, Suess D, Fox S, Harmer J, Driesener R, De La Paz L et al. X-ray crystallographic and EPR spectroscopic analysis of <i>hydG</i>, a maturase in [FeFe]-hydrogenase H-cluster assembly. Proceedings of the National Academy of Sciences. 2015;112(5):1362-1367.
 
<br><br>
 
<br><br>
−
[2] Pilet E, Nicolet Y, Mathevon C, Douki T, Fontecilla-Camps J, Fontecave M. The role of the maturase HydG in [FeFe]-hydrogenase active site synthesis and assembly. FEBS Letters. 2009;583(3):506-511.
+
[2] Pilet E, Nicolet Y, Mathevon C, Douki T, Fontecilla-Camps J, Fontecave M. The role of the maturase <i>hydG</i> in [FeFe]-hydrogenase active site synthesis and assembly. FEBS Letters. 2009;583(3):506-511.
 
<br><br>
 
<br><br>
 
[3] Posewitz M, King P, Smolinski S, Zhang L, Seibert M, Ghirardi M. Discovery of Two Novel Radical S-Adenosylmethionine Proteins Required for the Assembly of an Active [Fe] Hydrogenase. Journal of Biological Chemistry. 2004;279(24):25711-25720.
 
[3] Posewitz M, King P, Smolinski S, Zhang L, Seibert M, Ghirardi M. Discovery of Two Novel Radical S-Adenosylmethionine Proteins Required for the Assembly of an Active [Fe] Hydrogenase. Journal of Biological Chemistry. 2004;279(24):25711-25720.
 
<br><br>
 
<br><br>
−
[4] Driesener R, Duffus B, Shepard E, Bruzas I, Duschene K, Coleman N et al. Biochemical and Kinetic Characterization of Radical S -Adenosyl- l -methionine Enzyme HydG. Biochemistry. 2013;52(48):8696-8707
+
[4] Driesener R, Duffus B, Shepard E, Bruzas I, Duschene K, Coleman N et al. Biochemical and Kinetic Characterization of Radical S -Adenosyl- l -methionine Enzyme <i>hydG</i>. Biochemistry. 2013;52(48):8696-8707

Latest revision as of 13:15, 21 October 2016

HydG

Sequence and Features


Assembly Compatibility:
  • 10
    COMPATIBLE WITH RFC[10]
  • 12
    COMPATIBLE WITH RFC[12]
  • 21
    COMPATIBLE WITH RFC[21]
  • 23
    COMPATIBLE WITH RFC[23]
  • 25
    COMPATIBLE WITH RFC[25]
  • 1000
    COMPATIBLE WITH RFC[1000]


Overview

This part is composed of the hydG gene. All organisms with [Fe] hydrogenase and sequenced genomes contain homologues of hydE, hydF, and hydG. Within several prokaryotic genomes hydE, hydF, and hydG are found in putative operons with [Fe] hydrogenase structural genes.

HydrogenProduction

Biology & Literature

hydG is a radical S-adenosyl methionine (SAM) enzyme which catalyzes formation of a CO- and CN−-bound iron precursor to the H cluster, the cofactor on which [FeFe] hydrogenases are dependent on [1]. hydG breaks up the substrate tyrosine to yield both CO- and CN—ligands which act as precorsors during H-cluster assembly. It has been suggested that hydG cleaves the Cα–Cβ bond of tyrosine and p-cresol and dehydroglycine are formed as by-products [2]. hydE and hydF are maturases also required for the assembly of an active hydrogenase [3]. The binding site in hydG can accommodate either a [5Fe-5S] or a [4Fe-5S] cluster [4].

Protein information

hydG
Mass: 63.74kDa
Sequence:
MSVPLQCNAGRLLAGQRPCGVRARLNRRVCVPVTAHGKASATREYAGDFLPGTTISHAWSVERETHHRYRNPAEWINEAA IHKALETSKADAQDAGRVREILAKAKEKAFVTEHAPVNAESKSEFVQGLTLEECATLINVDSNNVELMNEIFDTALAIKE RIYGNRVVLFAPLYIANHCMNTCTYCAFRSANKGMERSILTDDDLREEVAALQRQGHRRILALTGEHPKYTFDNFLHAVN VIASVKTEPEGSIRRINVEIPPLSVSDMRRLKNTDSVGTFVLFQETYHRDTFKVMHPSGPKSDFDFRVLTQDRAMRAGLD DVGIGALFGLYDYRYEVCAMLMHSEHLEREYNAGPHTISVPRMRPADGSELSIAPPYPVNDADFMKLVAVLRIAVPYTGM ILSTRESPEMRSALLKCGMSQMSAGSRTDVGAYHKDHTLSTEANLSKLAGQFTLQDERPTNEIVKWLMEEGYVPSWCTAC YRQGRTGEDFMNICKAGDIHDFCHPNSLLTLQEYLMDYADPDLRKKGEQVIAREMGPDASEPLSAQSRKRLERKMKQVLE GEHDVYL

References

[1] Dinis P, Suess D, Fox S, Harmer J, Driesener R, De La Paz L et al. X-ray crystallographic and EPR spectroscopic analysis of hydG, a maturase in [FeFe]-hydrogenase H-cluster assembly. Proceedings of the National Academy of Sciences. 2015;112(5):1362-1367.

[2] Pilet E, Nicolet Y, Mathevon C, Douki T, Fontecilla-Camps J, Fontecave M. The role of the maturase hydG in [FeFe]-hydrogenase active site synthesis and assembly. FEBS Letters. 2009;583(3):506-511.

[3] Posewitz M, King P, Smolinski S, Zhang L, Seibert M, Ghirardi M. Discovery of Two Novel Radical S-Adenosylmethionine Proteins Required for the Assembly of an Active [Fe] Hydrogenase. Journal of Biological Chemistry. 2004;279(24):25711-25720.

[4] Driesener R, Duffus B, Shepard E, Bruzas I, Duschene K, Coleman N et al. Biochemical and Kinetic Characterization of Radical S -Adenosyl- l -methionine Enzyme hydG. Biochemistry. 2013;52(48):8696-8707