From Wikipedia, the free encyclopedia
Cyclic pyranopterin monophosphate synthase (
EC
4.1.99.18 , MOCS1A , MoaA , MoaC , molybdenum cofactor biosynthesis protein 1 ) is an
enzyme with
systematic name GTP 8,9-lyase (cyclic pyranopterin monophosphate-forming) .
[1]
[2]
[3]
[4]
[5]
[6]
[7] This enzyme
catalyses the following
chemical reaction
GTP
⇌
{\displaystyle \rightleftharpoons }
cyclic pyranopterin monophosphate +
diphosphate
This enzyme catalyses an early step in the
biosynthesis of
molybdopterin .
References
^ Rieder C, Eisenreich W, O'Brien J, Richter G, Götze E, Boyle P, Blanchard S, Bacher A, Simon H (July 1998). "Rearrangement reactions in the biosynthesis of molybdopterin--an NMR study with multiply 13C/15N labelled precursors". European Journal of Biochemistry . 255 (1): 24–36.
doi :
10.1046/j.1432-1327.1998.2550024.x .
PMID
9692897 .
^ Wuebbens MM, Rajagopalan KV (January 1995).
"Investigation of the early steps of molybdopterin biosynthesis in Escherichia coli through the use of in vivo labeling studies" . The Journal of Biological Chemistry . 270 (3): 1082–7.
doi :
10.1074/jbc.270.3.1082 .
PMID
7836363 .
^ Hänzelmann P, Hernández HL, Menzel C, García-Serres R, Huynh BH, Johnson MK, Mendel RR, Schindelin H (August 2004).
"Characterization of MOCS1A, an oxygen-sensitive iron-sulfur protein involved in human molybdenum cofactor biosynthesis" . The Journal of Biological Chemistry . 279 (33): 34721–32.
doi :
10.1074/jbc.M313398200 .
PMID
15180982 .
^ Hänzelmann P, Schindelin H (August 2004).
"Crystal structure of the S-adenosylmethionine-dependent enzyme MoaA and its implications for molybdenum cofactor deficiency in humans" . Proceedings of the National Academy of Sciences of the United States of America . 101 (35): 12870–5.
doi :
10.1073/pnas.0404624101 .
PMC
516487 .
PMID
15317939 .
^ Sanishvili R, Beasley S, Skarina T, Glesne D, Joachimiak A, Edwards A, Savchenko A (October 2004).
"The crystal structure of Escherichia coli MoaB suggests a probable role in molybdenum cofactor synthesis" . The Journal of Biological Chemistry . 279 (40): 42139–46.
doi :
10.1074/jbc.M407694200 .
PMC
3366512 .
PMID
15269205 .
^ Hänzelmann P, Schindelin H (May 2006).
"Binding of 5'-GTP to the C-terminal FeS cluster of the radical S-adenosylmethionine enzyme MoaA provides insights into its mechanism" . Proceedings of the National Academy of Sciences of the United States of America . 103 (18): 6829–34.
doi :
10.1073/pnas.0510711103 .
PMC
1458979 .
PMID
16632608 .
^ Lees NS, Hänzelmann P, Hernandez HL, Subramanian S, Schindelin H, Johnson MK, Hoffman BM (July 2009).
"ENDOR spectroscopy shows that guanine N1 binds to [4Fe-4S] cluster II of the S-adenosylmethionine-dependent enzyme MoaA: mechanistic implications" . Journal of the American Chemical Society . 131 (26): 9184–5.
doi :
10.1021/ja903978u .
PMC
2757093 .
PMID
19566093 .
External links
Activity Regulation Classification Kinetics Types