Difference between revisions of "Part:BBa K2740014"
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<h2>Design Notes</h2> | <h2>Design Notes</h2> | ||
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− | <p align="left">Nitrogenase is a complex enzyme system consisting of nine protein components. Additionally, to maintain stoichiometry of these protein components is an essential requirement for nitrogenase biosynthesis and activity. However, there is only one copy of each structure gene present in the nif gene cluster. Therefore, cloning each of these nif genes and setting as independent part can facilitate the regulation of balancing expression ratios from the transcription and/or translation level(s) when they are heterogeneously expressed in non-diazotrophic hosts | + | <p align="left">Nitrogenase is a complex enzyme system consisting of nine protein components. Additionally, to maintain stoichiometry of these protein components is an essential requirement for nitrogenase biosynthesis and activity. However, there is only one copy of each structure gene present in the nif gene cluster. Therefore, cloning each of these nif genes and setting as independent part can facilitate the regulation of balancing expression ratios from the transcription and/or translation level(s) when they are heterogeneously expressed in non-diazotrophic hosts.</p> |
Latest revision as of 10:14, 8 October 2018
CR1 nifD
CR1 nifD encodes the subunit alpha (NifD) of the molybdenum-iron (MoFe) protein.
Sequence and Features
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21COMPATIBLE WITH RFC[21]
- 23COMPATIBLE WITH RFC[23]
- 25COMPATIBLE WITH RFC[25]
- 1000COMPATIBLE WITH RFC[1000]
Parameter of Protein
Number of amino acids: 482
Molecular weight: 54204.38
Theoretical pI: 5.96
Amino acid composition:
Ala (A) 31 6.4%
Arg (R) 25 5.2%
Asn (N) 14 2.9%
Asp (D) 27 5.6%
Cys (C) 11 2.3%
Gln (Q) 15 3.1%
Glu (E) 39 8.1%
Gly (G) 47 9.8%
His (H) 13 2.7%
Ile (I) 41 8.5%
Leu (L) 29 6.0%
Lys (K) 33 6.8%
Met (M) 23 4.8%
Phe (F) 16 3.3%
Pro (P) 20 4.1%
Ser (S) 24 5.0%
Thr (T) 18 3.7%
Trp (W) 7 1.5%
Tyr (Y) 20 4.1%
Val (V) 29 6.0%
Pyl (O) 0 0.0%
Sec (U) 0 0.0%
(B) 0 0.0%
(Z) 0 0.0%
(X) 0 0.0%
Total number of negatively charged residues (Asp + Glu): 66
Total number of positively charged residues (Arg + Lys): 58
Atomic composition:
Carbon C 2405
Hydrogen H 3770
Nitrogen N 652
Oxygen O 706
Sulfur S 34
Formula: C2405H3770N652O706S34
Total number of atoms: 7567
Extinction coefficients:
Extinction coefficients are in units of M-1 cm-1, at 280 nm measured in water.
Ext. coefficient 68925
Abs 0.1% (=1 g/l) 1.272, assuming all pairs of Cys residues form cystines
Ext. coefficient 68300
Abs 0.1% (=1 g/l) 1.260, assuming all Cys residues are reduced
Estimated half-life:
The N-terminal of the sequence considered is M (Met).
The estimated half-life is: 30 hours (mammalian reticulocytes, in vitro).
>20 hours (yeast, in vivo).
>10 hours (Escherichia coli, in vivo).
Instability index:
The instability index (II) is computed to be 43.69
This classifies the protein as unstable.
Aliphatic index: 80.52
Grand average of hydropathicity (GRAVY): -0.294
Design Notes
Nitrogenase is a complex enzyme system consisting of nine protein components. Additionally, to maintain stoichiometry of these protein components is an essential requirement for nitrogenase biosynthesis and activity. However, there is only one copy of each structure gene present in the nif gene cluster. Therefore, cloning each of these nif genes and setting as independent part can facilitate the regulation of balancing expression ratios from the transcription and/or translation level(s) when they are heterogeneously expressed in non-diazotrophic hosts.