Sandbox Reserved 1501: Difference between revisions

Line 26:

The amino acid sequence in the heme binding region was first determined by Guidard ''et al'', 1974<ref>PMID: 4210211</ref>.

For every subunit of the wild type protein form, the crystallized preparation analysis determined a molecular weight of the chain of 36 kD (Appleby and Morton, 1959<ref>PMID: 13638255</ref>) and the chain of 21 kD (Jacq and Lederer, 1974<ref>PMID: 4152980</ref>).

The sulfite adduct recombinant enzyme produced when expressed in ''E. coli'' was also crystallized (Tegoni and Cambillau, 1994<ref>PMID: 8003966</ref>) so key active site residues could be identified and comparisons with the mutant protein.

The sulfite adduct recombinant enzyme produced when expressed in ''E. coli'' was also crystallized (Tegoni and Cambillau, 1994<ref name="bob">PMID: 8003966</ref>) so key active site residues could be identified and comparisons with the mutant protein.

The Arg289 of the ''E. coli'' wild type sulfite adduct can adopt two different conformations, one of which its side chain is stacked against Arg376, that directly interacts with the substrate, while in the second one the Arg289 side chain points towards the active site.

The mutation changes that Arg289 into a Lysine becoming R289K-b(2). The mutant ARG289LYS can still be found in both conformations but it is now changing the kinetics of the reactions (Tegoni and Cambillau, 1994<ref~~>PMID: 8003966<~~/~~ref~~>).

The mutation changes that Arg289 into a Lysine becoming R289K-b(2). The mutant ARG289LYS can still be found in both conformations but it is now changing the kinetics of the reactions (Tegoni and Cambillau, 1994<ref name="bob"/>).

It is rising the Ki of several components in comparison to the wild type, while kcat and KM are also changed by a factor of 10.

It changes also the induction by L-lactate. Patterns of inhibition by pyruvate and oxalate are altered and the enzyme stops being inhibited by substrate excess.

Sandbox Reserved 1501: Difference between revisions

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@@ Line 26: / Line 26: @@
 The amino acid sequence in the heme binding region was first determined by Guidard ''et al'', 1974<ref>PMID: 4210211</ref>.
 For every subunit of the wild type protein form, the crystallized preparation analysis determined a molecular weight of the chain of 36 kD (Appleby and Morton, 1959<ref>PMID: 13638255</ref>) and the chain of 21 kD (Jacq and Lederer, 1974<ref>PMID: 4152980</ref>).
-The sulfite adduct recombinant enzyme produced when expressed in ''E. coli'' was also crystallized (Tegoni and Cambillau, 1994<ref>PMID: 8003966</ref>) so key active site residues could be identified and comparisons with the mutant protein.
+The sulfite adduct recombinant enzyme produced when expressed in ''E. coli'' was also crystallized (Tegoni and Cambillau, 1994<ref name="bob">PMID: 8003966</ref>) so key active site residues could be identified and comparisons with the mutant protein.
 The Arg289 of the ''E. coli'' wild type sulfite adduct can adopt two different conformations, one of which its side chain is stacked against Arg376, that directly interacts with the substrate, while in the second one the Arg289 side chain points towards the active site.
-The mutation changes that Arg289 into a Lysine becoming R289K-b(2). The mutant ARG289LYS can still be found in both conformations but it is now changing the kinetics of the reactions (Tegoni and Cambillau, 1994<ref>PMID: 8003966</ref>).
+The mutation changes that Arg289 into a Lysine becoming R289K-b(2). The mutant ARG289LYS can still be found in both conformations but it is now changing the kinetics of the reactions (Tegoni and Cambillau, 1994<ref name="bob"/>).
 It is rising the K<sub>i</sub> of several components in comparison to the wild type, while k<sub>cat</sub> and K<sub>M</sub> are also changed by a factor of 10.
 It changes also the induction by L-lactate. Patterns of inhibition by pyruvate and oxalate are altered and the enzyme stops being inhibited by substrate excess.