engineering

Peptidylglycine monooxygenase

Peptidylglycine monooxygenase is a engineering topic covered in the lgStudy science library. This page brings together a partial reference excerpt, illustrations, worked examples, real-world applications and a short study plan, so you can understand Peptidylglycine monooxygenase rather than just read about it. In short: In enzymology, a peptidylglycine monooxygenase (EC 1.14.17.3) is an enzyme that catalyzes the chemical reaction peptidylglycine + ascorbate + O2 ⇌ {\displaystyle \rightleftharpoons } peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O The 3 substrates of this enzyme are peptidylglycine, ascorbate, and O2, whereas its 3 products are peptidyl(2-hydroxyglycine), dehydroascorbate, and H2O. This enzyme belongs to the fam…

Key takeaways

Peptidylglycine monooxygenase belongs to engineering; place it in that map before memorising details.
Learn the definition first, then one example that makes the definition concrete.
Connect Peptidylglycine monooxygenase to a quantity you can measure, compute or draw — that is where exam questions come from.
Reproduce the core statement of Peptidylglycine monooxygenase from memory before moving on to harder problems.

Reference excerpt

In enzymology, a peptidylglycine monooxygenase (EC 1.14.17.3) is an enzyme that catalyzes the chemical reaction

peptidylglycine + ascorbate + O2 ⇌ {\displaystyle \rightleftharpoons } peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O The 3 substrates of this enzyme are peptidylglycine, ascorbate, and O2, whereas its 3 products are peptidyl(2-hydroxyglycine), dehydroascorbate, and H2O. This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with reduced ascorbate as one donor, and incorporation of one atom of oxygen into the other donor. The systematic name of this enzyme class is peptidylglycine,ascorbate:oxygen oxidoreductase (2-hydroxylating). Other names in common use include 2-hydroxylase, alpha-amidating enzyme, peptide-alpha-amide synthetase, synthase, peptide alpha-amide, peptide alpha-amidating enzyme, peptide alpha-amide synthase, alpha-hydroxylase, alpha-amidating monooxygenase, PAM-A, PAM-B, and PAM. It employs one cofactor, copper.

Structural studies As of late 2007, 8 structures have been solved for this class of enzymes, with PDB accession codes PDB: 1OPM, PDB: 1PHM, PDB: 1SDW, PDB: 1YI9, PDB: 1YIP, PDB: 1YJK, PDB: 1YJL, and PDB: 3PHM.

References

Bradbury AF, Finnie MD, Smyth DG (1982). "Mechanism of C-terminal amide formation by pituitary enzymes". Nature. 298 (5875): 686–8. Bibcode:1982Natur.298..686B. doi:10.1038/298686a0. PMID 7099265. S2CID 4324776. Bradbury AF, Smyth DG (1987). "Enzyme-catalysed peptide amidation. Isolation of a stable intermediate formed by reaction of the amidating enzyme with an imino acid". Eur. J. Biochem. 169 (3): 579–84. doi:10.1111/j.1432-1033.1987.tb13648.x. PMID 3691506. Glembotski CC (1985). "Further characterization of the peptidyl alpha-amidating enzyme in rat anterior pituitary secretory granules". Arch. Biochem. Biophys. 241 (2): 673–83. doi:10.1016/0003-9861(85)90594-6. PMID 2994573. Katopodis AG, Ping D, May SW (1990). "A novel enzyme from bovine neurointermediate pituitary catalyzes dealkylation of alpha-hydroxyglycine derivatives, thereby functioning sequentially with peptidylglycine alpha-amidating monooxygenase in peptide amidation". Biochemistry. 29 (26): 6115–20. doi:10.1021/bi00478a001. PMID 2207061. Murthy AS, Keutmann HT, Eipper BA (1987). "Further characterization of peptidylglycine alpha-amidating monooxygenase from bovine neurointermediate pituitary". Mol. Endocrinol. 1 (4): 290–9. doi:10.1210/mend-1-4-290. PMID 3453894. Murthy AS, Mains RE, Eipper BA (1986). "Purification and characterization of peptidylglycine alpha-amidating monooxygenase from bovine neurointermediate pituitary". J. Biol. Chem. 261 (4): 1815–22. doi:10.1016/S0021-9258(17)36013-1. PMID 3944110.

Worked examples

Example 1 — a first encounter with Peptidylglycine monooxygenase

Start with the simplest possible case. Write down what Peptidylglycine monooxygenase claims or describes in one sentence, then invent the smallest concrete situation in which that sentence is true. In engineering, the smallest case is usually a single object, a single equation or a single measurement. Check that every symbol or term in your sentence has a meaning in that case.

Example 2 — changing one variable

Take the situation from Example 1 and change exactly one quantity: double it, halve it, or set it to zero. Predict what should happen to Peptidylglycine monooxygenase before you calculate. Comparing your prediction with the result is the fastest way to find out whether you understand the idea or only the words.

Example 3 — an exam-style question

Typical questions about Peptidylglycine monooxygenase ask you to (a) state it precisely, (b) apply it to given data, and (c) explain a limitation. Practise writing all three answers in under five minutes; the third part is what separates a full-mark answer from an average one.

Applications of Peptidylglycine monooxygenase

In research: Peptidylglycine monooxygenase appears in engineering research whenever the underlying quantities have to be modelled precisely. Papers usually cite it as a starting assumption and then explore where it breaks down.
In technology and industry: Engineering practice reuses Peptidylglycine monooxygenase in design rules, simulations and safety margins. Knowing the idea lets you read a specification sheet and understand why the numbers look the way they do.
In the classroom: Peptidylglycine monooxygenase is common in secondary-school and first-year university syllabi. It links to neighbouring topics Copper enzymes, EC 1.14.17, EC 1.14 stubs, so understanding it makes those chapters shorter.
In everyday life: Look for Peptidylglycine monooxygenase outside the textbook — in sport, cooking, traffic, electronics or the sky above you. An example you found yourself is remembered far longer than one you were given.

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Frequently asked questions

What is Peptidylglycine monooxygenase in simple terms?

In enzymology, a peptidylglycine monooxygenase (EC 1.14.17.3) is an enzyme that catalyzes the chemical reaction peptidylglycine + ascorbate + O2 ⇌ {\displaystyle \rightleftharpoons } peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O The 3 substrates of this enzyme are peptidylglycine, ascorbate…

Why does Peptidylglycine monooxygenase matter?

Because it connects several engineering ideas at once: it gives you a definition you can apply, a quantity you can calculate, and a way to check whether a result is plausible.

How should I study Peptidylglycine monooxygenase?

Read the excerpt, restate it from memory, then work through the examples and applications listed on this page. The five-step study plan above takes about twenty minutes.

What does this page cover?

It gives you a compact reference excerpt plus original lgStudy explanations, examples, applications and study material on Peptidylglycine monooxygenase.