Biochemistry flashcards work best when each card asks for one clear fact and makes you retrieve it before revealing the answer. This deck covers enzyme kinetics, carbohydrate and lipid metabolism, the urea cycle, haemoglobin and oxidative phosphorylation. It is a starting set for biomedical science revision, not a substitute for your course’s learning outcomes or notes.

How to work through this deck

Take each question in order. Try to answer it aloud or silently before you reveal the reverse. Compare your answer with the wording on the card, then grade your recall: choose Again if you could not retrieve the fact, Hard if you got it with difficulty, Good if you answered correctly, or Easy if it came quickly and accurately. Be strict about details such as direction of change, molecule names and quantities.

The grades help space out later reviews. A card you miss should return sooner; one you know securely can wait longer. Do not treat a familiar-looking question as proof of recall: answer it from memory before turning it. A MySummaries deck on this topic could look like this:

Cards — Biochemistry — core metabolism18 due

For Michaelis–Menten kinetics, what does Km represent?

The substrate concentration at which reaction velocity is half of Vmax.

All 18 cards
For Michaelis–Menten kinetics, what does Km represent?The substrate concentration at which reaction velocity is half of Vmax.
In competitive inhibition, what happens to apparent Km and Vmax?Apparent Km increases; Vmax is unchanged.
In pure non-competitive inhibition, what happens to Km and Vmax?Km is unchanged; Vmax decreases.
What is the net yield of glycolysis per glucose molecule?2 ATP and 2 NADH, with 2 pyruvate produced.
Name two activators and two inhibitors of phosphofructokinase-1 (PFK-1).AMP and fructose-2,6-bisphosphate activate it; ATP and citrate inhibit it.
Which five cofactors are used by the pyruvate dehydrogenase complex?Thiamine pyrophosphate, lipoate, coenzyme A, FAD and NAD+.
For each acetyl-CoA oxidised in the citric acid cycle, what is produced?3 NADH, 1 FADH2, 1 GTP and 2 CO2.
What is the terminal electron acceptor in the mitochondrial electron transport chain?Oxygen, which is reduced to water.
Which electron transport chain complex does not pump protons?Complex II, succinate dehydrogenase.
What directly drives ATP synthase during oxidative phosphorylation?The proton-motive force across the inner mitochondrial membrane.
How many beta-oxidation cycles and acetyl-CoA molecules result from palmitoyl-CoA?7 cycles yield 8 acetyl-CoA, plus 7 NADH and 7 FADH2.
What does glycogen phosphorylase release from glycogen?Glucose-1-phosphate from alpha-1,4 glycosidic bonds.
Which enzyme bypasses pyruvate kinase in gluconeogenesis?Pyruvate carboxylase and phosphoenolpyruvate carboxykinase act in sequence: pyruvate to oxaloacetate to phosphoenolpyruvate.
What activates carbamoyl phosphate synthetase I in the urea cycle?N-acetylglutamate.
What happens to the oxygen-binding curve of haemoglobin when 2,3-BPG increases?It shifts to the right, reducing haemoglobin's oxygen affinity.
Name three other factors that shift the haemoglobin oxygen-binding curve to the right.Increased H+ (lower pH), increased CO2 and increased temperature.
In anaerobic glycolysis, what does lactate dehydrogenase regenerate?NAD+ by reducing pyruvate to lactate.
Which vitamin cofactor is required by methylmalonyl-CoA mutase?Vitamin B12, in its adenosylcobalamin form.

That is a MySummaries deck, filled with biochemistry material. Yours is written from your own notes. Start free

The cards mix definitions, enzyme regulation, pathway yields and cause-and-effect. For each one, check whether you recalled the complete answer. For example, “competitive inhibition raises Km” is incomplete unless you also remember that Vmax remains unchanged. On the gluconeogenesis card, the bypass is a two-enzyme route, not a single replacement for pyruvate kinase.

Check the core before moving on

After the first pass, group the facts into pathways and ask whether you can explain the connection between them. Glycolysis produces pyruvate; when oxygen is limited, lactate dehydrogenase helps regenerate NAD+ so glycolysis can continue. In aerobic metabolism, pyruvate dehydrogenase links glycolysis to acetyl-CoA, which enters the citric acid cycle. The reducing equivalents then supply electrons to the respiratory chain.

A compact “Must not miss core” drawn from this deck might look like this:

Must not miss coreBiochemistry — core metabolism
Glycolysis per glucose: net 2 ATP, 2 NADH and 2 pyruvate; PFK-1 is activated by AMP and fructose-2,6-bisphosphate and inhibited by ATP and citrate.
Competitive inhibition: apparent Km rises and Vmax is unchanged; pure non-competitive inhibition: Km is unchanged and Vmax falls.
Per acetyl-CoA in the citric acid cycle: 3 NADH, 1 FADH2, 1 GTP and 2 CO2.
Palmitoyl-CoA beta-oxidation: 7 cycles yield 8 acetyl-CoA, 7 NADH and 7 FADH2.
Oxidative phosphorylation: oxygen is the terminal electron acceptor; the proton-motive force drives ATP synthase.

Use this short list as a retrieval check, not as a replacement for the cards. Cover the items with your hand or scroll past them, then say each one from memory. If an item is vague, return to the specific card and repair the missing detail. When your course uses a different level of pathway detail, add cards from your own lecture notes rather than assuming this core is exhaustive.

Repair repeated misses

A missed card is useful information: it points to a fact that needs another attempt. If you miss the same concept repeatedly, check whether the problem is recall or understanding. For instance, if you confuse Km and Vmax, draw a simple enzyme-rate graph and explain what changes when substrate concentration is plotted against velocity. Then review both inhibition cards again.

A remediation prompt can turn a repeated error into a precise next action. A MySummaries tray for this deck might contain:

Remediation tray

You lost this mark twice: for each acetyl-CoA entering the citric acid cycle, state the numbers of NADH, FADH2, GTP and CO2 produced.

Add cardDismiss

Answer the prompt, then check the relevant card and core item. If the answer is still incomplete, make a small comparison in your notes—for example, list the outputs per acetyl-CoA separately from the outputs per glucose. This prevents a correct pathway fact being applied at the wrong scale.

Review with spacing and context

Work through the deck in short sessions, revisiting due cards before adding many new ones. After a review, choose a few cards and connect them in a spoken explanation: regulation of glycolysis, the fate of pyruvate, or how electron transfer supports ATP synthesis. This tests whether isolated facts can be used together, while keeping the flashcards focused on one answer at a time.

Once these cards are secure, extend the deck from your own materials. Add the reaction direction, tissue context or clinical connection only where your course requires it, and keep each card answer narrow enough to grade reliably. For numerical yields, label the unit of comparison—per glucose, per acetyl-CoA or per fatty acid—so you do not memorise a number without its context.

How MySummaries helps

MySummaries builds revision boards from your own PDFs, slides and photographed notes, then turns board content into spaced-repetition cards. You can organise these biochemistry facts alongside your course material and review the cards that are due in MySummaries.