Coding

Part:BBa_K1998009

Designed by: Shauna Winchester   Group: iGEM16_Macquarie_Australia   (2016-10-13)
Revision as of 02:42, 21 October 2016 by SWinchester (Talk | contribs) (→‎Biology & Literature)


Hyd1

Sequence and Features


Assembly Compatibility:
  • 10
    COMPATIBLE WITH RFC[10]
  • 12
    INCOMPATIBLE WITH RFC[12]
    Illegal NheI site found at 157
  • 21
    COMPATIBLE WITH RFC[21]
  • 23
    COMPATIBLE WITH RFC[23]
  • 25
    COMPATIBLE WITH RFC[25]
  • 1000
    COMPATIBLE WITH RFC[1000]


Overview

HYD1 is an oxygen-tolerant hydrogenase; it is a respiratory enzyme that catalyses hydrogen oxidation. It has been suggested that it functions at more positive redox potentials, which are located at the aerobic-anaerobic interface. It forms one of the enzymes found in our hydrogenase pathway of our system.

HydrogenProduction

Biology & Literature

Hydrogenase 1 (Hyd1) is a gene which codes for a peptide containing 10 D-amino acids which has been known to induce cell autophagy resulting from an increase in reactive oxygen species and ATP depletion of the cell [1]. Hyd1 has also been known to help treat prostate cancer by preventing the adhesion of carcinomas to the epithelium lining of the digestive tract [1].

More specifically Hyd1 catalyses the oxidation of hydrogen in the anaerobic respiration of E.coli [2] this done by working in parallel with Hyd 2 before fermentation is undertaken by Hyd3 [2, 3]. Hyd1 is a membrane bound hydrogenase that facilitates the uptake of oxidated hydrogen gas [3]. The hya operon encodes the Hydrogenase peptide which is initiated under anaerobic conditions as well as acidic pH levels which signals that H+ must be facilitated to move from ICF to ECF and viceverser to maintain pH levels in E.coli [3, 4].

Part Verification

Fig 1. A gel consisting of EcorI/PstI double digests for the hydEF part (Lane 4) The hydEF (3611 bp) was observed as expected in the gel.

Protein information

Hyd1
Mass: 53.13 kDa
Sequence:
MSALVLKPCAAVSIRGSSCRARQVAPRAPLAASTVRVALATLEAPARRLGNVACAAAAPAAEAPLSHVQQALAELAKPKDDPTRKHVCVQVAPAVRVAIAETLGLAPGATT PKQLAEGLRRLGFDEVFDTLFGADLTIMEEGSELLHRLTEHLEAHPHSDEPLPMFTSCCPGWIAMLEKSYPDLIPYVSSCKSPQMMLAAMVKSYLAEKKGIAPKDMVMV SIMPCTRKQSEADRDWFCVDADPTLRQLDHVITTVELGNIFKERGINLAELPEGEWDNPMGVGSGAGVLFGTTGGVMEAALRTAYELFTGTPLPRLSLSEVRGMDGIKET NITMVPAPGSKFEELLKHRAAARAEAAAHGTPGPLAWDGGAGFTSEDGRGGITLRVAVANGLGNAKKLITKMQAGEAKYDFVEIMACPAGCVGGGGQPRSTDKAITQKR QAALYNLDEKSTLRRSHENPSIRELYDTYLGEPLGHKAHELLHTHYVAGGVEEKDEKK

References

[1] Nair RR, Emmons MF, Cress AE, Argilagos RF, Lam K, Kerr WT, Wang HG, Dalton WS, Hazlehurst LA. HYD1-induced increase in reactive oxygen species leads to autophagy and necrotic cell death in multiple myeloma cells. Molecular cancer therapeutics. 2009 Aug 1;8(8):2441-51.

[2] Redwood MD, Mikheenko IP, Sargent F, Macaskie LE. Dissecting the roles of Escherichia coli hydrogenases in biohydrogen production. FEMS microbiology letters. 2008 Jan 1;278(1):48-55.

[3] Bisaillon A, Turcot J, Hallenbeck PC. The effect of nutrient limitation on hydrogen production by batch cultures of Escherichia coli. International Journal of Hydrogen Energy. 2006 Sep 30;31(11):1504-8.

[4] Trchounian K, Trchounian A. Hydrogenase 2 is most and hydrogenase 1 is less responsible for H 2 production by Escherichia coli under glycerol fermentation at neutral and slightly alkaline pH. international journal of hydrogen energy. 2009 Nov 30;34(21):8839-45.

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