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Pterin - Pterin.svg
IUPAC names
(one of five tautomers)
Other names
3D model (JSmol)
ECHA InfoCard 100.017.091
Molar mass 163.137
Except where otherwise noted, data are given for materials in their standard state (at 25 °C [77 °F], 100 kPa).
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Infobox references

Pterin is a heterocyclic compound composed of a pteridine ring system, with a "keto group" (a lactam) and an amino group on positions 4 and 2 respectively. It is structurally related to the parent bicyclic heterocycle called pteridine. Pterins, as a group, are compounds related to pterin with additional substituents. Pterin itself is of no biological significance.

Pterins were first discovered in the pigments of butterfly wings[1] (hence the origin of their name, from the Greek pteron (πτερόν),[2] wing) and perform many roles in coloration in the biological world.

Pterin cofactors[edit]

One important family of pterin derivatives are Folates. Folates are pterins that contain p-aminobenzoic acid connected to the methyl group at position 6 of the pteridine ring system (known as pteroic acid) conjugated with one or more L-glutamates. They participate in numerous biological group transfer reactions. Folate-dependent biosynthetic reactions include the transfer of methyl groups from 5-methyltetrahydrofolate to homocysteine to form L-methionine, and the transfer of formyl groups from 10-formyltetrahydrofolate to L-methionine to form N-formylmethionine in initiator tRNAs. Folates are also essential for the biosynthesis of purines and one pyrimidine.

Molybdopterins are cofactors that are associated with almost all molybdenum-containing enzymes.


The biosynthesis of pterins begins with guanosine triphosphate (GTP), which is the substrate for GTP cyclohydrolase I.[3] The enzyme is found in both prokaryotes and eukaryotes.

step in biosynthesis of dihydroneopterin from GTP.

Molybdopterin biosynthesis occurs in four steps: (i) the radical-mediated cyclization of nucleotide, guanosine 5'-triphosphate (GTP), to (8S)‑3 ́,8‐cyclo‑7,8‑dihydroguanosine 5 ́‑triphosphate (3 ́,8‑cH2GTP), (ii) the formation of cyclic pyranopterin monophosphate (cPMP) from the 3 ́,8‑cH2GTP, (iii) the conversion of cPMP into molybdopterin (MPT), (iv) the insertion of molybdate into MPT to form Moco. The human enzymes are indicated in parenthesis.[4]

Moco biosynthetic pathway in bacteria and humans.

Other pterins[edit]

Pterin can exist in many different forms in nature depending on its function. Tetrahydrobiopterin (BH4), the major unconjugated pteridine in vertebrates, is a co-factor in the hydroxylation of aromatic compounds and synthesis of nitric oxide. Molybdopterin is a substituted pteridine that binds molybdenum to yield redox cofactors involved in biological hydroxylations, reduction of nitrate, and respiratory oxidation. Tetrahydromethanopterin is used in methanogenic organisms.[5] Cyanopterin is a glycosylated version of pteridine of unknown function in cyanobacteria.

The wings of the orange tip butterfly are colored by orange pterin-containing pigments.[6]

See also[edit]


  1. ^ Wijnen B1, Leertouwer HL, Stavenga DG. Colors and pterin pigmentation of pierid butterfly wings. J Insect Physiol. 2007 Dec;53(12):1206-17. Epub 2007 Jul 1
  2. ^ πτερόν. Liddell, Henry George; Scott, Robert; A Greek–English Lexicon at the Perseus Project
  3. ^ J. Rebelo, G. Auerbach, G Bader, A. Bracher, H. Nar, C. Hösl, N. Schramek, J. Kaiser, A. Bacher, R. Huber, M. Fischer (2003). "Biosynthesis of Pteridines. Reaction Mechanism of GTP Cyclohydrolase I". J. Mol. Biol. 326: 503–516. doi:10.1016/S0022-2836(02)01303-7. 
  4. ^ Schwarz, G. & Mendel, R. R. (2006). "Molybdenum cofactor biosynthesis and molybdenum enzymes". Annual Review of Plant Biology. 57: 623–647. doi:10.1146/annurev.arplant.57.032905.105437. PMID 16669776. 
  5. ^ Schwarz, Guenter; Mendel, Ralf R.; Ribbe, Markus W. (2009). "Molybdenum cofactors, enzymes and pathways". From Nature. 460: 839–847. doi:10.1038/nature08302. 
  6. ^ B. Wijnen, H. L. Leertouwer, D. G.Stavenga (2007). "Colors and pterin pigmentation of pierid butterfly wings". Journal of Insect Physiology. 53: 1206–1217. doi:10.1016/j.jinsphys.2007.06.016. 


External links[edit]