Enzymes
| UniProtKB help_outline | 5,552 proteins |
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- Name help_outline siroheme Identifier CHEBI:60052 Charge -8 Formula C42H36FeN4O16 InChIKeyhelp_outline DLKSSIHHLYNIKN-QIISWYHFSA-D SMILEShelp_outline C[C@]1(CC([O-])=O)[C@H](CCC([O-])=O)C2=CC3=[N+]4C(=Cc5c(CC([O-])=O)c(CCC([O-])=O)c6C=C7C(CCC([O-])=O)=C(CC([O-])=O)C8=[N+]7[Fe--]4(N2C1=C8)n56)[C@@H](CCC([O-])=O)[C@]3(C)CC([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 2 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline H+ Identifier CHEBI:15378 Charge 1 Formula H InChIKeyhelp_outline GPRLSGONYQIRFK-UHFFFAOYSA-N SMILEShelp_outline [H+] 2D coordinates Mol file for the small molecule Search links Involved in 9,717 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline sirohydrochlorin Identifier CHEBI:58351 Charge -8 Formula C42H38N4O16 InChIKeyhelp_outline KWIZRXMMFRBUML-AHGFGAHVSA-F SMILEShelp_outline C[C@]1(CC([O-])=O)[C@H](CCC([O-])=O)c2cc3[nH]c(cc4nc(cc5[nH]c(cc1n2)c(CC([O-])=O)c5CCC([O-])=O)c(CCC([O-])=O)c4CC([O-])=O)[C@@H](CCC([O-])=O)[C@]3(C)CC([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 4 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline Fe2+ Identifier CHEBI:29033 (CAS: 15438-31-0) help_outline Charge 2 Formula Fe InChIKeyhelp_outline CWYNVVGOOAEACU-UHFFFAOYSA-N SMILEShelp_outline [Fe++] 2D coordinates Mol file for the small molecule Search links Involved in 266 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:24360 | RHEA:24361 | RHEA:24362 | RHEA:24363 | |
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| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
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Publications
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The biosynthesis of adenosylcobalamin (vitamin B12).
Warren M.J., Raux E., Schubert H.L., Escalante-Semerena J.C.
Vitamin B12, or cobalamin, is one of the most structurally complex small molecules made in Nature. Major progress has been made over the past decade in understanding how this synthesis is accomplished. This review covers some of the most important findings that have been made and provides the read ... >> More
Vitamin B12, or cobalamin, is one of the most structurally complex small molecules made in Nature. Major progress has been made over the past decade in understanding how this synthesis is accomplished. This review covers some of the most important findings that have been made and provides the reader with a complete description of the transformation of uroporphyrinogen III into adenosylcobalamin (AdoCbl). 183 references are cited. << Less
Nat Prod Rep 19:390-412(2002) [PubMed] [EuropePMC]
This publication is cited by 16 other entries.
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The structure of Saccharomyces cerevisiae Met8p, a bifunctional dehydrogenase and ferrochelatase.
Schubert H.L., Raux E., Brindley A.A., Leech H.K., Wilson K.S., Hill C.P., Warren M.J.
Sirohaem is a tetrapyrrole-derived prosthetic group that is required for the essential assimilation of sulfur and nitrogen into all living systems as part of the sulfite and nitrite reductase systems. The final two steps in the biosynthesis of sirohaem involve a beta-NAD(+)-dependent dehydrogenati ... >> More
Sirohaem is a tetrapyrrole-derived prosthetic group that is required for the essential assimilation of sulfur and nitrogen into all living systems as part of the sulfite and nitrite reductase systems. The final two steps in the biosynthesis of sirohaem involve a beta-NAD(+)-dependent dehydrogenation of precorrin-2 to generate sirohydrochlorin followed by ferrochelation to yield sirohaem. In Saccharomyces cerevisiae, Met8p is a bifunctional enzyme that carries out both of these reactions. Here, we report the 2.2 A resolution crystal structure of Met8p, which adopts a novel fold that bears no resemblance to the previously determined structures of cobalt- or ferro-chelatases. Analysis of mutant proteins suggests that both catalytic activities share a single active site, and that Asp141 plays an essential role in both dehydrogenase and chelatase processes. << Less
EMBO J. 21:2068-2075(2002) [PubMed] [EuropePMC]
This publication is cited by 4 other entries.