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===Usage and Biology=== | ===Usage and Biology=== | ||
During heme biosynthesis, this enzyme catalyses the asymmetric cyclization of linear tetrapyrrole to form a uroporphyrinogen III isomer. At the catalytic site, hydroxymethylbilane use as a substrate gives uroporphyrinogen III[1]. Reports have identified that along with hemA and hemL, upregulation of hemD and hemF increases the 5-Aminolevulinic acid accumulation which is a promising source for cancer treatment[2]. | During heme biosynthesis, this enzyme catalyses the asymmetric cyclization of linear tetrapyrrole to form a uroporphyrinogen III isomer. At the catalytic site, hydroxymethylbilane use as a substrate gives uroporphyrinogen III[1]. Reports have identified that along with hemA and hemL, upregulation of hemD and hemF increases the 5-Aminolevulinic acid accumulation which is a promising source for cancer treatment[2]. | ||
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===References=== | ===References=== | ||
1. Schubert, H. L., Phillips, J. D., Heroux, A., & Hill, C. P. (2008). Structure and Mechanistic Implications of a Uroporphyrinogen III Synthase−Product Complex. Biochemistry, 47(33), 8648–8655. | 1. Schubert, H. L., Phillips, J. D., Heroux, A., & Hill, C. P. (2008). Structure and Mechanistic Implications of a Uroporphyrinogen III Synthase−Product Complex. Biochemistry, 47(33), 8648–8655. | ||
Revision as of 19:43, 21 October 2021
hemD
This is an enzyme involved in the heme biosynthetic pathway. Also called uroporphyrinogen III synthase.
IISER_Bhopal 2021
Usage and Biology
During heme biosynthesis, this enzyme catalyses the asymmetric cyclization of linear tetrapyrrole to form a uroporphyrinogen III isomer. At the catalytic site, hydroxymethylbilane use as a substrate gives uroporphyrinogen III[1]. Reports have identified that along with hemA and hemL, upregulation of hemD and hemF increases the 5-Aminolevulinic acid accumulation which is a promising source for cancer treatment[2].
References
1. Schubert, H. L., Phillips, J. D., Heroux, A., & Hill, C. P. (2008). Structure and Mechanistic Implications of a Uroporphyrinogen III Synthase−Product Complex. Biochemistry, 47(33), 8648–8655.
2. Zhang, J., Kang, Z., Chen, J., & Du, G. (2015). Optimization of the heme biosynthesis pathway for the production of 5-aminolevulinic acid in Escherichia coli. Scientific Reports, 5(1).
Sequence and Features
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21COMPATIBLE WITH RFC[21]
- 23COMPATIBLE WITH RFC[23]
- 25COMPATIBLE WITH RFC[25]
- 1000COMPATIBLE WITH RFC[1000]