Heme A (YMDB00882)

Identification
YMDB IDYMDB00882
NameHeme A
SpeciesSaccharomyces cerevisiae
StrainBaker's yeast
DescriptionHeme a is a derivative of protoheme IX (heme b or heme). Heme a differs from heme b in that a methyl side chain at ring position 8 is oxidized into a formyl group, and one of the vinyl side chains, at ring position 2, has been replaced by an isoprenoid chain. In the heme biosynthesis from uroporphyrinogen-III pathway, different derivatives of protoheme can actually be formed that differ in modifications to the porphyrin ring, including how it is bound to the protein (e.g. heme o, heme a, heme c, and heme d). [Biocyc PWY-5189]
Structure
Thumb
MOLSDFPDBSMILESInChI
Synonyms
  • (SP-4-2)[7-ethenyl-17-formyl-12-[(4E,8E)-1-hydroxy-5,9,13-trimethyl-4,8,12-tetradecatrienyl]-3,8,13-trimethyl-21H,23H-porphine-2,18-dipropanoato(4-)-kappaN21,kappaN22,kappaN23,kappaN24]-Ferrate(2-)
  • [SP-4-2-(E,E)]-[7-ethenyl-17-formyl-12-(1-hydroxy-5,9,13-trimethyl-4,8,12-tetradecatrienyl)-3,8,13-trimethyl-21H,23H-porphine-2,18-dipropanoato(4-)-N21,N22,N23,N24]-Ferrate(2-)
  • Heme a
CAS number57560-10-8
WeightAverage: 852.837
Monoisotopic: 852.354927677
InChI KeyKZGQHTJCCRPHLY-AXLBWSHISA-N
InChIInChI=1S/C49H56N4O6.Fe/c1-9-34-31(6)39-25-45-49(46(55)18-12-17-30(5)16-11-15-29(4)14-10-13-28(2)3)33(8)40(52-45)24-44-37(27-54)36(20-22-48(58)59)43(53-44)26-42-35(19-21-47(56)57)32(7)38(51-42)23-41(34)50-39;/h9,13,15,17,23-27,46,55H,1,10-12,14,16,18-22H2,2-8H3,(H,56,57)(H,58,59);/q-2;+4/b29-15+,30-17+,38-23-,40-24-,42-26-,45-25-;
IUPAC Name4,20-bis(2-carboxyethyl)-15-ethenyl-5-formyl-10-[(4E,8E)-1-hydroxy-5,9,13-trimethyltetradeca-4,8,12-trien-1-yl]-9,14,19-trimethyl-2lambda5,22,23lambda5,25-tetraaza-1-ferraoctacyclo[11.9.1.1^{1,8}.1^{3,21}.0^{2,6}.0^{16,23}.0^{18,22}.0^{11,25}]pentacosa-2,4,6,8,10,12,14,16(23),17,19,21(24)-undecaene-2,23-bis(ylium)
Traditional IUPAC Name4,20-bis(2-carboxyethyl)-15-ethenyl-5-formyl-10-[(4E,8E)-1-hydroxy-5,9,13-trimethyltetradeca-4,8,12-trien-1-yl]-9,14,19-trimethyl-2lambda5,22,23lambda5,25-tetraaza-1-ferraoctacyclo[11.9.1.1^{1,8}.1^{3,21}.0^{2,6}.0^{16,23}.0^{18,22}.0^{11,25}]pentacosa-2,4,6,8,10,12,14,16(23),17,19,21(24)-undecaene-2,23-bis(ylium)
Chemical FormulaC49H56FeN4O6
SMILES[H]OC(=O)C([H])([H])C([H])([H])C1=C(C2=C([H])C3=[N]4C(=C([H])C5=C(C(=C6C([H])=C7C(C([H])=O)=C(C8=[N]7[Fe++]4(N2C1=C8[H])N56)C([H])([H])C([H])([H])C(=O)O[H])C([H])([H])[H])C([H])(O[H])C([H])([H])C([H])([H])C([H])=C(C([H])([H])[H])C([H])([H])C([H])([H])C([H])=C(C([H])([H])[H])C([H])([H])C([H])([H])C([H])=C(C([H])([H])[H])C([H])([H])[H])C(=C3C([H])=C([H])[H])C([H])([H])[H])C([H])([H])[H]
Chemical Taxonomy
Description belongs to the class of organic compounds known as metallotetrapyrroles. These are polycyclic compounds containing a tetrapyrrole skeleton combined with a metal atom.
KingdomOrganic compounds
Super ClassOrganoheterocyclic compounds
ClassTetrapyrroles and derivatives
Sub ClassMetallotetrapyrroles
Direct ParentMetallotetrapyrroles
Alternative ParentsNot Available
SubstituentsNot Available
Molecular FrameworkNot Available
External DescriptorsNot Available
Physical Properties
StateSolid
Charge2
Melting pointNot Available
Experimental Properties
PropertyValueReference
Water SolubilityNot AvailablePhysProp
LogPNot AvailablePhysProp
Predicted Properties
PropertyValueSource
Water Solubility0.00021 g/LALOGPS
logP2.16ALOGPS
logP4.58ChemAxon
logS-6.6ALOGPS
pKa (Strongest Acidic)3.2ChemAxon
pKa (Strongest Basic)-3.1ChemAxon
Physiological Charge0ChemAxon
Hydrogen Acceptor Count6ChemAxon
Hydrogen Donor Count3ChemAxon
Polar Surface Area129.52 ŲChemAxon
Rotatable Bond Count18ChemAxon
Refractivity244.19 m³·mol⁻¹ChemAxon
Polarizability100.2 ųChemAxon
Number of Rings8ChemAxon
Bioavailability0ChemAxon
Rule of FiveYesChemAxon
Ghose FilterYesChemAxon
Veber's RuleYesChemAxon
MDDR-like RuleYesChemAxon
Biological Properties
Cellular Locations
  • mitochondrion
Organoleptic PropertiesNot Available
SMPDB Pathways
Porphyrin MetabolismPW002462 ThumbThumb?image type=greyscaleThumb?image type=simple
KEGG Pathways
Porphyrin and chlorophyll metabolismec00860 Map00860
SMPDB Reactions
Heme O → Heme A
KEGG Reactions
NADH + heme o + oxygen → NAD + Heme A + water
Concentrations
Intracellular ConcentrationsNot Available
Extracellular ConcentrationsNot Available
Spectra
SpectraNot Available
References
References:
  • Herrgard, M. J., Swainston, N., Dobson, P., Dunn, W. B., Arga, K. Y., Arvas, M., Bluthgen, N., Borger, S., Costenoble, R., Heinemann, M., Hucka, M., Le Novere, N., Li, P., Liebermeister, W., Mo, M. L., Oliveira, A. P., Petranovic, D., Pettifer, S., Simeonidis, E., Smallbone, K., Spasic, I., Weichart, D., Brent, R., Broomhead, D. S., Westerhoff, H. V., Kirdar, B., Penttila, M., Klipp, E., Palsson, B. O., Sauer, U., Oliver, S. G., Mendes, P., Nielsen, J., Kell, D. B. (2008). "A consensus yeast metabolic network reconstruction obtained from a community approach to systems biology." Nat Biotechnol 26:1155-1160.18846089
  • Buchensky, C., Almiron, P., Mantilla, B. S., Silber, A. M., Cricco, J. A. (2010). "The Trypanosoma cruzi proteins TcCox10 and TcCox15 catalyze the formation of heme A in the yeast Saccharomyces cerevisiae." FEMS Microbiol Lett 312:133-141.20979346
Synthesis Reference:Not Available
External Links:
ResourceLink
CHEBI ID24479
HMDB IDHMDB06901
Pubchem Compound ID23724533
Kegg IDC15670
ChemSpider IDNot Available
FOODB IDFDB024148
WikipediaHeme_A
BioCyc IDHEME_A

Enzymes

Protein Details
1. Cytochrome c oxidase assembly protein COX15
General function:
Involved in protein complex assembly
Specific function:
Required for the assembly of yeast cytochrome oxidase. Involved in the biosynthesis of heme A and the initial step in this pathway, the hydroxylation of heme O, is thought to be catalyzed by a three-component mono-oxygenase consisting of COX15, ferredoxin and ferredoxin reductase
Gene Name:
COX15
Uniprot ID:
P40086
Molecular weight:
54657.89844