MOCS2

MOCS2
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
Aliases MOCS2, MCBPE, MOCO1, MOCODB, MPTS, molybdenum cofactor synthesis 2
External IDs MGI: 1336894 HomoloGene: 32193 GeneCards: MOCS2
RNA expression pattern
More reference expression data
Orthologs
Species Human Mouse
Entrez

4338

17434

Ensembl

ENSG00000164172

ENSMUSG00000015536

UniProt

O96007
O96033

Q9Z223
Q9Z224

RefSeq (mRNA)

NM_176806
NM_004531

NM_001113374
NM_001113375
NM_013826

RefSeq (protein)

NP_004522.1
NP_789776.1

NP_001106845.1
NP_038854.2

Location (UCSC) Chr 5: 53.1 – 53.11 Mb Chr 13: 114.82 – 114.83 Mb
PubMed search [1] [2]
Wikidata
View/Edit HumanView/Edit Mouse

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.[3][4][5] These two proteins dimerize to form molybdopterin synthase.

Function

Eukaryotic molybdoenzymes use a unique molybdenum cofactor (MoCo) consisting of a pterin, termed molybdopterin, and the catalytically active metal molybdenum. MoCo is synthesized from cyclic pyranopterin monophosphate (precursor Z) by the heterodimeric enzyme molybdopterin synthase.[5]

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.[5]

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

Genetic disease

Defects in both copies of MOCS2 cause the molybdenum cofactor deficiency disease in babies.[6]

Protein Structure

MOCS2A and MOCS2B subunits form dimers in solution. These dimers in turn dimerize to form the tetrameric molybdopterin synthase complex.[7]

References

  1. "Human PubMed Reference:".
  2. "Mouse PubMed Reference:".
  3. 1 2 Reiss J, Dorche C, Stallmeyer B, Mendel RR, Cohen N, Zabot MT (March 1999). "Human molybdopterin synthase gene: genomic structure and mutations in molybdenum cofactor deficiency type B". American Journal of Human Genetics. 64 (3): 706–11. doi:10.1086/302296. PMC 1377787Freely accessible. PMID 10053004.
  4. Sloan J, Kinghorn JR, Unkles SE (February 1999). "The two subunits of human molybdopterin synthase: evidence for a bicistronic messenger RNA with overlapping reading frames". Nucleic Acids Research. 27 (3): 854–8. doi:10.1093/nar/27.3.854. PMC 148257Freely accessible. PMID 9889283.
  5. 1 2 3 EntrezGene 4338: MOCS2 molybdenum cofactor synthesis 2
  6. Ichida K, Aydin HI, Hosoyamada M, et al. (2006). "A Turkish case with molybdenum cofactor deficiency". Nucleosides, Nucleotides & Nucleic Acids. 25 (9–11): 1087–91. doi:10.1080/15257770600894022. PMID 17065069.
  7. Leimkuhler S, Freuer A, Araujo JA, Rajagopalan KV, Mendel RR (July 2003). "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. doi:10.1074/jbc.M303092200. PMID 12732628.

Further reading


This article is issued from Wikipedia - version of the 6/2/2016. The text is available under the Creative Commons Attribution/Share Alike but additional terms may apply for the media files.