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% Document Info
\author{ilsccsonoa (holscassidy)}
\pdfinfo{
  /Title (metabolism.pdf)
  /Creator (Cheatography)
  /Author (ilsccsonoa (holscassidy))
  /Subject (metabolism Cheat Sheet)
}

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\noindent
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    {\parbox{\dimexpr\textwidth-2\fboxsep\relax}{\noindent
        \hspace*{-6pt}\includegraphics[width=5.8cm]{/web/www.cheatography.com/public/images/cheatography_logo.pdf}}
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\begin{tabulary}{11cm}{L}
    \vspace{-2pt}\large{\bf{\textcolor{DarkBackground}{\textrm{metabolism Cheat Sheet}}}} \\
    \normalsize{by \textcolor{DarkBackground}{ilsccsonoa (holscassidy)} via \textcolor{DarkBackground}{\uline{cheatography.com/185549/cs/39061/}}}
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\noindent
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  \mymulticolumn{2}{p{5.377cm}}{\bf\textcolor{white}{Cheatographer}}  \\
  \vspace{-2pt}ilsccsonoa (holscassidy) \\
  \uline{cheatography.com/holscassidy} \\
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  \mymulticolumn{1}{p{5.377cm}}{\bf\textcolor{white}{Cheat Sheet}}  \\
   \vspace{-2pt}Not Yet Published.\\
   Updated 3rd June, 2023.\\
   Page {\thepage} of \pageref{LastPage}.
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  \vspace{-5pt}
  %\includegraphics[width=48px,height=48px]{dave.jpeg}
  Measure your website readability!\\
  www.readability-score.com
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\begin{document}
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\begin{multicols*}{3}

\begin{tabularx}{5.377cm}{X}
\SetRowColor{DarkBackground}
\mymulticolumn{1}{x{5.377cm}}{\bf\textcolor{white}{enzyme-driven reactions}}  \tn
% Row 0
\SetRowColor{LightBackground}
\mymulticolumn{1}{x{5.377cm}}{break down food to produce energy (catabolism), stored as ATP \& electron carriers: NADH, NADPH2, FADH2} \tn 
% Row Count 3 (+ 3)
% Row 1
\SetRowColor{white}
\mymulticolumn{1}{x{5.377cm}}{build up from biomolecules (anabolism), requiring energy in form of phosphoryl group transfer from ATP \& reducing power of NADH \& NADPH} \tn 
% Row Count 6 (+ 3)
% Row 2
\SetRowColor{LightBackground}
\mymulticolumn{1}{x{5.377cm}}{eliminate waste} \tn 
% Row Count 7 (+ 1)
% Row 3
\SetRowColor{white}
\mymulticolumn{1}{x{5.377cm}}{grow \& reproduce, maintain structures \& respond to environment} \tn 
% Row Count 9 (+ 2)
% Row 4
\SetRowColor{LightBackground}
\mymulticolumn{1}{x{5.377cm}}{drive desirable energy-requiring reactions by coupling them to spontaneous energy-releasing reactions} \tn 
% Row Count 12 (+ 3)
\hhline{>{\arrayrulecolor{DarkBackground}}-}
\end{tabularx}
\par\addvspace{1.3em}

\begin{tabularx}{5.377cm}{X}
\SetRowColor{DarkBackground}
\mymulticolumn{1}{x{5.377cm}}{\bf\textcolor{white}{glycolysis}}  \tn
% Row 0
\SetRowColor{LightBackground}
\mymulticolumn{1}{x{5.377cm}}{cytoplasm} \tn 
% Row Count 1 (+ 1)
% Row 1
\SetRowColor{white}
\mymulticolumn{1}{x{5.377cm}}{1. phosphate group transferred from ATP to glucose-6-phosphate. Catalysed by hexokinase. 1 molecule of ATP used} \tn 
% Row Count 4 (+ 3)
% Row 2
\SetRowColor{LightBackground}
\mymulticolumn{1}{x{5.377cm}}{2. Glucose-6-phosphate converted to isomer fructose-6-phosphate by phosphoglucose isomerase enzyme} \tn 
% Row Count 6 (+ 2)
% Row 3
\SetRowColor{white}
\mymulticolumn{1}{x{5.377cm}}{3. second ATP molecule used to phosphorylate fructose-6-phosphate to produce fructose-1,6-bisphosphate. catalysed by phosphofructokinase.} \tn 
% Row Count 9 (+ 3)
% Row 4
\SetRowColor{LightBackground}
\mymulticolumn{1}{x{5.377cm}}{4. fructose 1,6-bisphosphate is split into 2x 3C sugars by adolase. these are \seqsplit{glyceraldehyde-3-phosphate} \& dihydroxyacetone phosphate} \tn 
% Row Count 12 (+ 3)
% Row 5
\SetRowColor{white}
\mymulticolumn{1}{x{5.377cm}}{5. DHAP converted to GAP by triose phosphate isomerase} \tn 
% Row Count 14 (+ 2)
% Row 6
\SetRowColor{LightBackground}
\mymulticolumn{1}{x{5.377cm}}{6. G3P dehydrogenase enzyme catalyses two processes: it oxidises GAP, \& at the same time NAD+ is reduced to NADH + H+. overall reaction releases energy that is used to phosphorylate GAP, creating 2 x 1,3-bisphosphoglycerate molecules.} \tn 
% Row Count 19 (+ 5)
% Row 7
\SetRowColor{white}
\mymulticolumn{1}{x{5.377cm}}{7. each of the two BPG molecules donate a phosphate group to an ADP, forming 2 x ATP \& two molecules of 3-phosphoglycerate. catalysed by phosphoglycerate kinase.} \tn 
% Row Count 23 (+ 4)
% Row 8
\SetRowColor{LightBackground}
\mymulticolumn{1}{x{5.377cm}}{8. phosphoglyceromutase converts two 3 PGA into 2 molecules of 2-phosphoglycerate (isomers)} \tn 
% Row Count 25 (+ 2)
% Row 9
\SetRowColor{white}
\mymulticolumn{1}{x{5.377cm}}{9. enolase removes a water molecule from each of 2PGA, creating two molecules of phosphoenolpyruvate} \tn 
% Row Count 27 (+ 2)
% Row 10
\SetRowColor{LightBackground}
\mymulticolumn{1}{x{5.377cm}}{10. phosphate group transferred from PEP to ADP, creating 2 x ATP \& 2x pyruvate. catalysed by pyruvate kinase.} \tn 
% Row Count 30 (+ 3)
\hhline{>{\arrayrulecolor{DarkBackground}}-}
\end{tabularx}
\par\addvspace{1.3em}

\begin{tabularx}{5.377cm}{X}
\SetRowColor{DarkBackground}
\mymulticolumn{1}{x{5.377cm}}{\bf\textcolor{white}{glycosis notes}}  \tn
\SetRowColor{white}
\mymulticolumn{1}{x{5.377cm}}{1. 6th c is phosphorylated as it is the most exposed. neg charge addition of phosphate prevents g6p from leaving cytosol. Delta g negative \& irreversible.  \newline % Row Count 4 (+ 4)
2. isomerisation rearranges atoms to present another C for phosphorylation. delta g 0, reversible. \newline % Row Count 6 (+ 2)
3. delta g negative \& irreversible. \newline % Row Count 7 (+ 1)
4. lysis. previous phosphates added makes fructose easier to break due to charge redistribution. products used up quickly, pushing equil to right. delta g positive \& irreversible. \newline % Row Count 11 (+ 4)
5. isomerisation moves carbonyl to generate g3p which is more reactive. delta g positive \& reversible. \newline % Row Count 14 (+ 3)
6. redox generates highly reactive acyl phosphate intermediate \& NADH. enzyme is dehydrogenase because it takes H off first C. Delta g 0, reversible. \newline % Row Count 17 (+ 3)
7. sub-level phosphorylation. delta g large, neg \& irreversible. \newline % Row Count 19 (+ 2)
8. isomerisation moves phosphate from 3rd to 2nd position to make molecule more reactive, delta g 0, reversible. \newline % Row Count 22 (+ 3)
9. dehydration. delta g 0, reversible. \newline % Row Count 23 (+ 1)
10. sub-level phosphorylation. delta g negative \& irreversible.% Row Count 25 (+ 2)
} \tn 
\hhline{>{\arrayrulecolor{DarkBackground}}-}
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\begin{tabularx}{5.377cm}{X}
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\mymulticolumn{1}{x{5.377cm}}{\bf\textcolor{white}{anaerobic reduction of pyruvate to lactate}}  \tn
% Row 0
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\mymulticolumn{1}{x{5.377cm}}{during vigorous exercise, pyuvate production \textgreater{} pyruvate oxidation (by citric acid cycle)} \tn 
% Row Count 2 (+ 2)
% Row 1
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\mymulticolumn{1}{x{5.377cm}}{red blood cells lack mitochondria, produce lactate} \tn 
% Row Count 3 (+ 1)
% Row 2
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\mymulticolumn{1}{x{5.377cm}}{the 2x NADH are oxidised to 2x NAD+ by lactate dehydrogenase to regenerate NAD+ \& maintain redox balance} \tn 
% Row Count 6 (+ 3)
\hhline{>{\arrayrulecolor{DarkBackground}}-}
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\begin{tabularx}{5.377cm}{X}
\SetRowColor{DarkBackground}
\mymulticolumn{1}{x{5.377cm}}{\bf\textcolor{white}{Gibbs free energy}}  \tn
% Row 0
\SetRowColor{LightBackground}
\mymulticolumn{1}{x{5.377cm}}{amount of free energy available is related to the difference in energy levels between products \& reactions} \tn 
% Row Count 3 (+ 3)
% Row 1
\SetRowColor{white}
\mymulticolumn{1}{x{5.377cm}}{if +/- 10 kj/mol = at equil} \tn 
% Row Count 4 (+ 1)
% Row 2
\SetRowColor{LightBackground}
\mymulticolumn{1}{x{5.377cm}}{if over 10 kj/mol = favours substrate, little product} \tn 
% Row Count 6 (+ 2)
% Row 3
\SetRowColor{white}
\mymulticolumn{1}{x{5.377cm}}{if under - 10 kj/mol = favours product, little substrate} \tn 
% Row Count 8 (+ 2)
\hhline{>{\arrayrulecolor{DarkBackground}}-}
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\begin{tabularx}{5.377cm}{X}
\SetRowColor{DarkBackground}
\mymulticolumn{1}{x{5.377cm}}{\bf\textcolor{white}{TCA cycle}}  \tn
% Row 0
\SetRowColor{LightBackground}
\mymulticolumn{1}{x{5.377cm}}{Can Intelligent Karen Solve Some Foreign Mafia Operations?} \tn 
% Row Count 2 (+ 2)
% Row 1
\SetRowColor{white}
\mymulticolumn{1}{x{5.377cm}}{Link: pyruvate from glycolysis is decarboxylated to form acetyl-CoA by pyruvate dehydrogenase.} \tn 
% Row Count 4 (+ 2)
% Row 2
\SetRowColor{LightBackground}
\mymulticolumn{1}{x{5.377cm}}{1. (condensation), acetyl-CoA (2C) joins oxalocetate (4C) to form citrate (6c) + CoA. catalysed by citrate synthase. delta G neg \& irr.} \tn 
% Row Count 7 (+ 3)
% Row 3
\SetRowColor{white}
\mymulticolumn{1}{x{5.377cm}}{2. citrate converted to isocitrate isomer. catalysed by aconitase. dehydration \& hydration step alter position of H/OH. delta G positive \& irr.} \tn 
% Row Count 10 (+ 3)
% Row 4
\SetRowColor{LightBackground}
\mymulticolumn{1}{x{5.377cm}}{3. isocitrate oxidised to alpha-ketoglutarate (5C) resulting in release of CO2. 1 x NADH2 molecule formed. catalysed by isocitrate dehydrogenase.} \tn 
% Row Count 13 (+ 3)
% Row 5
\SetRowColor{white}
\mymulticolumn{1}{x{5.377cm}}{4. alpha-ketoglutarate oxidised to form 4C molecule succinate that binds to CoA forming succinal CoA. catalysed by alpha-ketoglutarate dehydrogenase complex. 2nd NADH produced \& 2nd O2. delta G = neg \& irr.} \tn 
% Row Count 18 (+ 5)
% Row 6
\SetRowColor{LightBackground}
\mymulticolumn{1}{x{5.377cm}}{5. succinyl coA to succinate (4C) \& one GTP produced. catalysed by succinylchlorine-CoA synthetase. delta g = 0 \& rev} \tn 
% Row Count 21 (+ 3)
% Row 7
\SetRowColor{white}
\mymulticolumn{1}{x{5.377cm}}{6. succinate to fumerate (4C) \& molecule of FADH2 produced. delta G = 0 \& rev. catalysed by succinate dehydrogenase.} \tn 
% Row Count 24 (+ 3)
% Row 8
\SetRowColor{LightBackground}
\mymulticolumn{1}{x{5.377cm}}{7. fumarate to malate (4C). hydration, catalysed by fumerase. delta G =0, reversible.} \tn 
% Row Count 26 (+ 2)
% Row 9
\SetRowColor{white}
\mymulticolumn{1}{x{5.377cm}}{8. malate to oxaloacetate, 3rd NADH produced. dehydrogenation to make oxaloacetate to keep cycle going. catalysed by malate dehydrogenase. delta G = pos \& irr.} \tn 
% Row Count 30 (+ 4)
\hhline{>{\arrayrulecolor{DarkBackground}}-}
\SetRowColor{LightBackground}
\mymulticolumn{1}{x{5.377cm}}{cycle occurs twice - one for each pyruvate}  \tn 
\hhline{>{\arrayrulecolor{DarkBackground}}-}
\end{tabularx}
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\begin{tabularx}{5.377cm}{X}
\SetRowColor{DarkBackground}
\mymulticolumn{1}{x{5.377cm}}{\bf\textcolor{white}{oxidative phosphorylation: e- transport chain}}  \tn
% Row 0
\SetRowColor{LightBackground}
\mymulticolumn{1}{x{5.377cm}}{NADH, FADH2 have electrons in high energy states that move from NADH, FADH2, reducing O2 to H2O \& energy is transferred to protein complexes} \tn 
% Row Count 3 (+ 3)
% Row 1
\SetRowColor{white}
\mymulticolumn{1}{x{5.377cm}}{Energy from oxidising NADH, FADH2 used to pump H+s into intermembrane space} \tn 
% Row Count 5 (+ 2)
% Row 2
\SetRowColor{LightBackground}
\mymulticolumn{1}{x{5.377cm}}{Intermembrane space more acidic than matrix – creates electrochemical gradient} \tn 
% Row Count 7 (+ 2)
% Row 3
\SetRowColor{white}
\mymulticolumn{1}{x{5.377cm}}{Flow of H+s down electrochemical gradient used to generate ATP} \tn 
% Row Count 9 (+ 2)
% Row 4
\SetRowColor{LightBackground}
\mymulticolumn{1}{x{5.377cm}}{electron transfer with transfer of H+ protons across inner mitochondria membrane used to create electrochemical gradient \& generate ATP} \tn 
% Row Count 12 (+ 3)
\hhline{>{\arrayrulecolor{DarkBackground}}-}
\end{tabularx}
\par\addvspace{1.3em}

\begin{tabularx}{5.377cm}{X}
\SetRowColor{DarkBackground}
\mymulticolumn{1}{x{5.377cm}}{\bf\textcolor{white}{end products}}  \tn
\SetRowColor{LightBackground}
\mymulticolumn{1}{p{5.377cm}}{\vspace{1px}\centerline{\includegraphics[width=5.1cm]{/web/www.cheatography.com/public/uploads/holscassidy_1685783622_Screen Shot 2023-06-03 at 10.13.10.png}}} \tn 
\hhline{>{\arrayrulecolor{DarkBackground}}-}
\end{tabularx}
\par\addvspace{1.3em}


% That's all folks
\end{multicols*}

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