Difference between revisions of "Part:BBa I716155"
(→‎IISER_Bhopal 2021)
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===Usage and Biology===
 
===Usage and Biology===
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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]. Guocheng Du et al. group 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].
 
===References===
 
===References===
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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. https://doi.org/10.1021/bi800635y
+
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.  
  
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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). https://doi.org/10.1038/srep08584
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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).  
  
 
<span class='h3bb'>Sequence and Features</span>
 
<span class='h3bb'>Sequence and Features</span>

Revision as of 14:16, 9 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


Assembly Compatibility:
  • 10
    COMPATIBLE WITH RFC[10]
  • 12
    COMPATIBLE WITH RFC[12]
  • 21
    COMPATIBLE WITH RFC[21]
  • 23
    COMPATIBLE WITH RFC[23]
  • 25
    COMPATIBLE WITH RFC[25]
  • 1000
    COMPATIBLE WITH RFC[1000]