MOCS2

Generic protein structure example

Molybdenum cofactor synthesis protein 2A and molybdenum cofactor synthesis protein 2B are a pair of proteins that in humans are encoded from the same MOCS2 gene.[1][2][3] These two proteins dimerize to form molybdopterin synthase.

## Contents

* 1 Function
* 2 Gene
* 2.1 Genetic disease
* 3 Protein structure
* 4 References
* 5 Further reading

## Function

Eukaryotic molybdoenzymes use a unique molybdenum cofactor (MoCo) consisting of a pterin and the catalytically active metal molybdenum. MoCo is synthesized from cyclic pyranopterin monophosphate (precursor Z) by the heterodimeric enzyme molybdopterin synthase.[3]

## Gene

The large and small subunits of molybdopterin synthase are both encoded from the MOCS2 gene by overlapping open reading frames. The proteins were initially thought to be encoded from a bicistronic transcript. They are now thought to be encoded from monocistronic transcripts. Alternatively spliced transcripts have been found for this locus that encode the large and small subunits.[3]

The MOCS2 gene contains 7 exons. Exons 1 to 3 encode MOCS2A (the small subunit), and exons 3 to 7 encode MOCS2B (large subunit).[1]

### Genetic disease

Defects in both copies of MOCS2 cause the molybdenum cofactor deficiency disease in babies.[4]

## Protein structure

MOCS2A and MOCS2B subunits form dimers in solution. These dimers in turn dimerize to form the tetrameric molybdopterin synthase complex.[5]

## References

1. ↑ 1.0 1.1 "Human molybdopterin synthase gene: genomic structure and mutations in molybdenum cofactor deficiency type B". American Journal of Human Genetics 64 (3): 706–11. March 1999. doi:10.1086/302296. PMID 10053004.
2. ↑ "The two subunits of human molybdopterin synthase: evidence for a bicistronic messenger RNA with overlapping reading frames". Nucleic Acids Research 27 (3): 854–8. February 1999. doi:10.1093/nar/27.3.854. PMID 9889283.
3. ↑ 3.0 3.1 3.2 EntrezGene 4338: MOCS2 molybdenum cofactor synthesis 2
4. ↑ "A Turkish case with molybdenum cofactor deficiency". Nucleosides, Nucleotides & Nucleic Acids 25 (9–11): 1087–91. 2006. doi:10.1080/15257770600894022. PMID 17065069.
5. ↑ "Mechanistic studies of human molybdopterin synthase reaction and characterization of mutants identified in group B patients of molybdenum cofactor deficiency". The Journal of Biological Chemistry 278 (28): 26127–34. July 2003. doi:10.1074/jbc.M303092200. PMID 12732628.

## Further reading

* "Mutations in the molybdenum cofactor biosynthetic genes MOCS1, MOCS2, and GEPH". Human Mutation 21 (6): 569–76. June 2003. doi:10.1002/humu.10223. PMID 12754701.
* "The mutational spectrum of single base-pair substitutions in mRNA splice junctions of human genes: causes and consequences". Human Genetics 90 (1–2): 41–54. 1992. doi:10.1007/bf00210743. PMID 1427786.
* "Mutations in a polycistronic nuclear gene associated with molybdenum cofactor deficiency". Nature Genetics 20 (1): 51–3. September 1998. doi:10.1038/1706. PMID 9731530.
* "Dual requirement for gephyrin in glycine receptor clustering and molybdoenzyme activity". Science 282 (5392): 1321–4. November 1998. doi:10.1126/science.282.5392.1321. PMID 9812897.
* "Human molybdopterin synthase gene: identification of a bicistronic transcript with overlapping reading frames". American Journal of Human Genetics 64 (3): 698–705. March 1999. doi:10.1086/302295. PMID 10053003.
* "Molybdopterin synthase mutations in a mild case of molybdenum cofactor deficiency". American Journal of Medical Genetics 104 (2): 169–73. November 2001. doi:10.1002/1096-8628(20011122)104:2<169::AID-AJMG1603>3.0.CO;2-8. PMID 11746050.
* "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proceedings of the National Academy of Sciences of the United States of America 99 (26): 16899–903. December 2002. doi:10.1073/pnas.242603899. PMID 12477932.
* "Evidence for the physiological role of a rhodanese-like protein for the biosynthesis of the molybdenum cofactor in humans". Proceedings of the National Academy of Sciences of the United States of America 101 (16): 5946–51. April 2004. doi:10.1073/pnas.0308191101. PMID 15073332.
* "The Status, Quality, and Expansion of the NIH Full-Length cDNA Project: The Mammalian Gene Collection (MGC)". Genome Research 14 (10B): 2121–7. October 2004. doi:10.1101/gr.2596504. PMID 15489334.
* "Ten novel mutations in the molybdenum cofactor genes MOCS1 and MOCS2 and in vitro characterization of a MOCS2 mutation that abolishes the binding ability of molybdopterin synthase". Human Genetics 117 (6): 565–70. October 2005. doi:10.1007/s00439-005-1341-9. PMID 16021469.
* "A novel MOCS2 mutation reveals coordinated expression of the small and large subunit of molybdopterin synthase". Molecular Genetics and Metabolism 89 (3): 210–3. November 2006. doi:10.1016/j.ymgme.2006.04.008. PMID 16737835.
* "A probability-based approach for high-throughput protein phosphorylation analysis and site localization". Nature Biotechnology 24 (10): 1285–92. October 2006. doi:10.1038/nbt1240. PMID 16964243.
* "Molybdenum cofactor deficiency: clinical features in a Turkish patient". Brain & Development 29 (6): 365–8. July 2007. doi:10.1016/j.braindev.2006.10.007. PMID 17158010.

* v
* t
* e

Metabolism of vitamins, coenzymes, and cofactors

Fat soluble vitamins|

| Vitamin A|

* Retinol binding protein

|

Vitamin E|

* Alpha-tocopherol transfer protein

Vitamin D|

* liver (Sterol 27-hydroxylase or CYP27A1)
* renal (25-Hydroxyvitamin D3 1-alpha-hydroxylase or CYP27B1)
* degradation (1,25-Dihydroxyvitamin D3 24-hydroxylase or CYP24A1)

Vitamin K|

* Vitamin K epoxide reductase

Water soluble vitamins|

| Thiamine (B1)|

* Thiamine diphosphokinase

|

Niacin (B3)|

* Indoleamine 2,3-dioxygenase
* Formamidase

Pantothenic acid (B5)|

* Pantothenate kinase

Folic acid (B9)|

* Dihydropteroate synthase
* Dihydrofolate reductase
* Serine hydroxymethyltransferase

* Methylenetetrahydrofolate reductase

Vitamin B12|

* MMAA
* MMAB
* MMACHC
* MMADHC

Vitamin C|

* L-gulonolactone oxidase

Riboflavin (B2)|

* Riboflavin kinase

Nonvitamin cofactors|

| Tetrahydrobiopterin|

* GTP cyclohydrolase I
* 6-pyruvoyltetrahydropterin synthase
* Sepiapterin reductase

* PCBD1
* PTS
* QDPR

Molybdenum cofactor|

* MOCS1
* MOCS2
* MOCS3
* Gephyrin

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