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Record Information

Version

2.0

Creation Date

2012-05-31 13:44:54 -0600

Update Date

2015-06-03 15:53:43 -0600

Secondary Accession Numbers

ECMDB01086

Identification

Name:

Uroporphyrinogen III

Description

Uroporphyrinogens are porphyrinogen variants in which each pyrrole ring has one acetate side chain and one propionate side chain; it is formed by condensation 4 four molecules of porphobilinogen. 4 isomers are possible but only 2 commoly are found, types I and III. Uroporphyrinogen III is a functional intermediate in heme biosynthesis while Uroporphyrinogen I is produced in an abortive side reaction.

Structure

MOL SDF PDB SMILES InChI

Synonyms:

3,8,13,17-Tetrakis(carboxymethyl)-5,10,15,20,22,24-hexahydro-2,7,12,18-Porphinetetrapropionate
3,8,13,17-Tetrakis(carboxymethyl)-5,10,15,20,22,24-hexahydro-2,7,12,18-Porphinetetrapropionic acid
3,8,13,17-Tetrakis(carboxymethyl)-5,10,15,20,22,24-hexahydro-21H,23H-Porphine-2,7,12,18-tetrapropanoate
3,8,13,17-Tetrakis(carboxymethyl)-5,10,15,20,22,24-hexahydro-21H,23H-Porphine-2,7,12,18-tetrapropanoic acid
3,8,13,17-Tetrakis(carboxymethyl)-5,10,15,20,22,24-hexahydroporphyrin-2,7,12,18-tetrapropanoate
3,8,13,17-Tetrakis(carboxymethyl)-5,10,15,20,22,24-hexahydroporphyrin-2,7,12,18-tetrapropanoic acid
Urogen I
Urogen III
UroPorgen-III
Uroporphyrinogen I
Uroporphyrinogen III
Uroporphyrinogen-III

Chemical Formula:

C₄₀H₄₄N₄O₁₆

Weight:

Average: 836.7946
Monoisotopic: 836.27523138

InChI Key:

HUHWZXWWOFSFKF-UHFFFAOYSA-N

InChI:

InChI=1S/C40H44N4O16/c45-33(46)5-1-17-21(9-37(53)54)29-14-27-19(3-7-35(49)50)22(10-38(55)56)30(43-27)15-28-20(4-8-36(51)52)24(12-40(59)60)32(44-28)16-31-23(11-39(57)58)18(2-6-34(47)48)26(42-31)13-25(17)41-29/h41-44H,1-16H2,(H,45,46)(H,47,48)(H,49,50)(H,51,52)(H,53,54)(H,55,56)(H,57,58)(H,59,60)

CAS number:

1976-85-8

IUPAC Name:

3-[9,14,20-tris(2-carboxyethyl)-5,10,15,19-tetrakis(carboxymethyl)-21,22,23,24-tetraazapentacyclo[16.2.1.1³,⁶.1⁸,¹¹.1¹³,¹⁶]tetracosa-1(20),3,5,8,10,13,15,18-octaen-4-yl]propanoic acid

Traditional IUPAC Name:

uroporphyrinogen-III

SMILES:

OC(=O)CCC1=C2CC3=C(CCC(O)=O)C(CC(O)=O)=C(CC4=C(CC(O)=O)C(CCC(O)=O)=C(CC5=C(CC(O)=O)C(CCC(O)=O)=C(CC(N2)=C1CC(O)=O)N5)N4)N3

Chemical Taxonomy

Description

belongs to the class of organic compounds known as porphyrins. Porphyrins are compounds containing a fundamental skeleton of four pyrrole nuclei united through the alpha-positions by four methine groups to form a macrocyclic structure.

Kingdom

Organic compounds

Super Class

Organoheterocyclic compounds

Class

Tetrapyrroles and derivatives

Sub Class

Porphyrins

Direct Parent

Porphyrins

Alternative Parents

Substituents

Porphyrin
Substituted pyrrole
Pyrrole
Heteroaromatic compound
Carboxylic acid derivative
Carboxylic acid
Azacycle
Carbonyl group
Hydrocarbon derivative
Organic oxide
Organopnictogen compound
Organooxygen compound
Organonitrogen compound
Organic oxygen compound
Organic nitrogen compound
Aromatic heteropolycyclic compound

Molecular Framework

Aromatic heteropolycyclic compounds

External Descriptors

uroporphyrinogen (CHEBI:15437 )

Physical Properties

State:

Solid

Charge:

-8

Melting point:

Not Available

Experimental Properties:

Property	Value	Source

Predicted Properties

Property	Value	Source
Water Solubility	0.044 g/L	ALOGPS
logP	0.67	ALOGPS
logP	1.39	ChemAxon
logS	-4.3	ALOGPS
pKa (Strongest Acidic)	3.21	ChemAxon
Physiological Charge	-8	ChemAxon
Hydrogen Acceptor Count	16	ChemAxon
Hydrogen Donor Count	12	ChemAxon
Polar Surface Area	361.56 Å²	ChemAxon
Rotatable Bond Count	20	ChemAxon
Refractivity	206.93 m³·mol⁻¹	ChemAxon
Polarizability	81.55 Å³	ChemAxon
Number of Rings	5	ChemAxon
Bioavailability	0	ChemAxon
Rule of Five	Yes	ChemAxon
Ghose Filter	Yes	ChemAxon
Veber's Rule	Yes	ChemAxon
MDDR-like Rule	Yes	ChemAxon

Biological Properties

Cellular Locations:

Cytoplasm

Reactions:

SMPDB Pathways:

Porphyrin metabolism

PW000936

KEGG Pathways:

Metabolic pathways eco01100
Porphyrin and chlorophyll metabolism ec00860

EcoCyc Pathways:

heme biosynthesis from uroporphyrinogen-III I HEME-BIOSYNTHESIS-II
heme biosynthesis from uroporphyrinogen-III II HEMESYN2-PWY
siroheme biosynthesis PWY-5194
superpathway of heme biosynthesis from uroporphyrinogen-III PWY0-1415
tetrapyrrole biosynthesis I PWY-5188

Concentrations

Not Available

Spectra

Spectra:

Spectrum Type	Description	Splash Key
Predicted LC-MS/MS	Predicted LC-MS/MS Spectrum - 10V, Positive	splash10-106r-0000000980-8aa242b9a95e3ad92890	View in MoNA
Predicted LC-MS/MS	Predicted LC-MS/MS Spectrum - 20V, Positive	splash10-05fr-0000000910-5ea901953b2295eabfb6	View in MoNA
Predicted LC-MS/MS	Predicted LC-MS/MS Spectrum - 40V, Positive	splash10-0ab9-0000000900-fe3587925504317b1a70	View in MoNA
Predicted LC-MS/MS	Predicted LC-MS/MS Spectrum - 10V, Negative	splash10-00xr-0000000930-6a464d08b50b7b5e266c	View in MoNA
Predicted LC-MS/MS	Predicted LC-MS/MS Spectrum - 20V, Negative	splash10-00di-0000000910-22d2fcd94b453076587d	View in MoNA
Predicted LC-MS/MS	Predicted LC-MS/MS Spectrum - 40V, Negative	splash10-00di-2000000900-342f06471315f49e3deb	View in MoNA
Predicted LC-MS/MS	Predicted LC-MS/MS Spectrum - 10V, Positive	splash10-00xr-0000000950-9b8035c556d329d65d92	View in MoNA
Predicted LC-MS/MS	Predicted LC-MS/MS Spectrum - 20V, Positive	splash10-008a-0000000900-ca31eaf24646ca5e9004	View in MoNA
Predicted LC-MS/MS	Predicted LC-MS/MS Spectrum - 40V, Positive	splash10-0032-0000000900-42e2c47ece780e68ce9c	View in MoNA
Predicted LC-MS/MS	Predicted LC-MS/MS Spectrum - 10V, Negative	splash10-00dj-0000000900-efbf6751227445074375	View in MoNA
Predicted LC-MS/MS	Predicted LC-MS/MS Spectrum - 20V, Negative	splash10-0002-0000000900-1faa99e113ce7b175d67	View in MoNA
Predicted LC-MS/MS	Predicted LC-MS/MS Spectrum - 40V, Negative	splash10-00kb-0000000900-479f518906c52f496e89	View in MoNA
MS	Mass Spectrum (Electron Ionization)	Not Available	View in JSpectraViewer
1D NMR	13C NMR Spectrum	Not Available	View in JSpectraViewer
1D NMR	1H NMR Spectrum	Not Available	View in JSpectraViewer
1D NMR	13C NMR Spectrum	Not Available	View in JSpectraViewer
1D NMR	1H NMR Spectrum	Not Available	View in JSpectraViewer
1D NMR	13C NMR Spectrum	Not Available	View in JSpectraViewer
1D NMR	1H NMR Spectrum	Not Available	View in JSpectraViewer
1D NMR	13C NMR Spectrum	Not Available	View in JSpectraViewer
1D NMR	1H NMR Spectrum	Not Available	View in JSpectraViewer
1D NMR	13C NMR Spectrum	Not Available	View in JSpectraViewer
1D NMR	1H NMR Spectrum	Not Available	View in JSpectraViewer
1D NMR	13C NMR Spectrum	Not Available	View in JSpectraViewer
1D NMR	1H NMR Spectrum	Not Available	View in JSpectraViewer
1D NMR	13C NMR Spectrum	Not Available	View in JSpectraViewer
1D NMR	1H NMR Spectrum	Not Available	View in JSpectraViewer
1D NMR	13C NMR Spectrum	Not Available	View in JSpectraViewer
1D NMR	1H NMR Spectrum	Not Available	View in JSpectraViewer
1D NMR	13C NMR Spectrum	Not Available	View in JSpectraViewer
1D NMR	1H NMR Spectrum	Not Available	View in JSpectraViewer
1D NMR	13C NMR Spectrum	Not Available	View in JSpectraViewer
1D NMR	1H NMR Spectrum	Not Available	View in JSpectraViewer

References

References:

Aizencang G, Solis C, Bishop DF, Warner C, Desnick RJ: Human uroporphyrinogen-III synthase: genomic organization, alternative promoters, and erythroid-specific expression. Genomics. 2000 Dec 1;70(2):223-31. Pubmed: 11112350
Kanehisa, M., Goto, S., Sato, Y., Furumichi, M., Tanabe, M. (2012). "KEGG for integration and interpretation of large-scale molecular data sets." Nucleic Acids Res 40:D109-D114. Pubmed: 22080510
Keseler, I. M., Collado-Vides, J., Santos-Zavaleta, A., Peralta-Gil, M., Gama-Castro, S., Muniz-Rascado, L., Bonavides-Martinez, C., Paley, S., Krummenacker, M., Altman, T., Kaipa, P., Spaulding, A., Pacheco, J., Latendresse, M., Fulcher, C., Sarker, M., Shearer, A. G., Mackie, A., Paulsen, I., Gunsalus, R. P., Karp, P. D. (2011). "EcoCyc: a comprehensive database of Escherichia coli biology." Nucleic Acids Res 39:D583-D590. Pubmed: 21097882
Martins BM, Grimm B, Mock HP, Huber R, Messerschmidt A: Crystal structure and substrate binding modeling of the uroporphyrinogen-III decarboxylase from Nicotiana tabacum. Implications for the catalytic mechanism. J Biol Chem. 2001 Nov 23;276(47):44108-16. Epub 2001 Aug 27. Pubmed: 11524417
van der Werf, M. J., Overkamp, K. M., Muilwijk, B., Coulier, L., Hankemeier, T. (2007). "Microbial metabolomics: toward a platform with full metabolome coverage." Anal Biochem 370:17-25. Pubmed: 17765195
Winder, C. L., Dunn, W. B., Schuler, S., Broadhurst, D., Jarvis, R., Stephens, G. M., Goodacre, R. (2008). "Global metabolic profiling of Escherichia coli cultures: an evaluation of methods for quenching and extraction of intracellular metabolites." Anal Chem 80:2939-2948. Pubmed: 18331064

Synthesis Reference:

Not Available

Material Safety Data Sheet (MSDS)

Not Available

Links

External Links:

Resource	Link
CHEBI ID	15437
HMDB ID	HMDB01086
Pubchem Compound ID	1179
Kegg ID	C01051
ChemSpider ID	1146
Wikipedia	Uroporphyrinogen III
BioCyc ID	UROPORPHYRINOGEN-III
EcoCyc ID	UROPORPHYRINOGEN-III
Ligand Expo	UP2

Enzymes

Protein Details

1. Uroporphyrinogen-III synthase

General function:: Involved in uroporphyrinogen-III synthase activity
Specific function:: Catalyzes cyclization of the linear tetrapyrrole, hydroxymethylbilane, to the macrocyclic uroporphyrinogen III
Gene Name:: hemD
Uniprot ID:: P09126
Molecular weight:: 27798

Reactions

Hydroxymethylbilane = uroporphyrinogen III + H(2)O.

Protein Details

2. Putative uroporphyrinogen-III C-methyltransferase

General function:: Coenzyme transport and metabolism
Specific function:: S-adenosyl-L-methionine + uroporphyrinogen III = S-adenosyl-L-homocysteine + precorrin-1
Gene Name:: hemX
Uniprot ID:: P09127
Molecular weight:: 42963

Reactions

S-adenosyl-L-methionine + uroporphyrinogen III = S-adenosyl-L-homocysteine + precorrin-1.
S-adenosyl-L-methionine + precorrin-1 = S-adenosyl-L-homocysteine + precorrin-2.

Protein Details

3. Siroheme synthase

General function:: Involved in methyltransferase activity
Specific function:: Multifunctional enzyme that catalyzes the SAM-dependent methylation of uroporphyrinogen III at position C-2 and C-7 to form precorrin-2 and then position C-12 or C-18 to form trimethylpyrrocorphin 2. It also catalyzes the conversion of precorrin-2 into siroheme. This reaction consists of the NAD- dependent oxidation of precorrin-2 into sirohydrochlorin and its subsequent ferrochelation into siroheme
Gene Name:: cysG
Uniprot ID:: P0AEA8
Molecular weight:: 49951

Reactions

S-adenosyl-L-methionine + uroporphyrinogen III = S-adenosyl-L-homocysteine + precorrin-1.
S-adenosyl-L-methionine + precorrin-1 = S-adenosyl-L-homocysteine + precorrin-2.
Precorrin-2 + NAD(+) = sirohydrochlorin + NADH.
Siroheme + 2 H(+) = sirohydrochlorin + Fe(2+).

Protein Details

4. Uroporphyrinogen decarboxylase

General function:: Involved in uroporphyrinogen decarboxylase activity
Specific function:: Catalyzes the decarboxylation of four acetate groups of uroporphyrinogen-III to yield coproporphyrinogen-III
Gene Name:: hemE
Uniprot ID:: P29680
Molecular weight:: 39248

Reactions

Uroporphyrinogen III = coproporphyrinogen + 4 CO(2).

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Uroporphyrinogen III (M2MDB000248)

Structure for #<Compound:0xaeceb004>

Enzymes

Reactions

Reactions

Reactions

Reactions