In molecular biology, the IMPDH/GMPR family of enzymes includes IMP dehydrogenase and GMP reductase. These enzymes are involved in purine metabolism. These enzymes adopt a TIM barrel structure.[1][2]
| IMP dehydrogenase / GMP reductase domain | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 binary complex of human type-i inosine monophosphate dehydrogenase with 6-cl-imp | |||||||||
| Identifiers | |||||||||
| Symbol | IMPDH | ||||||||
| Pfam | PF00478 | ||||||||
| Pfam clan | CL0036 | ||||||||
| InterPro | IPR001093 | ||||||||
| PROSITE | PDOC00391 | ||||||||
| SCOP2 | 1ak5 / SCOPe / SUPFAM | ||||||||
| |||||||||
References edit
- ^ Whitby FG, Luecke H, Kuhn P, Somoza JR, Huete-Perez JA, Phillips JD, et al. (1997). "Crystal structure of Tritrichomonas foetus inosine-5'-monophosphate dehydrogenase and the enzyme-product complex". Biochemistry. 36 (35): 10666–74. doi:10.1021/bi9708850. PMID 9271497.
- ^ Zhang R, Evans G, Rotella FJ, Westbrook EM, Beno D, Huberman E, et al. (1999). "Characteristics and crystal structure of bacterial inosine-5'-monophosphate dehydrogenase". Biochemistry. 38 (15): 4691–700. doi:10.1021/bi982858v. PMID 10200156.
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