Any feedback?
No. of entries
Information on EC 1.14.14.B10 - heme oxygenase (hematinic acid-producing)
for references in articles please use BRENDA:EC1.14.14.B10
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Old data from external sources may still be available.
Please check here for current data: EC unknown
Please check here for current data: EC unknown
preliminary BRENDA-supplied EC number
EC Tree 1 Oxidoreductases
1.14 Acting on paired donors, with incorporation or reduction of molecular oxygen
1.14.14 With reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen into the other donor
1.14.14.B10 heme oxygenase (hematinic acid-producing)
The expected taxonomic range for this enzyme is: Escherichia coli
showSynonyms
ChuS, heme oxygenase 1, HO-1, more
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
ChuS
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
heme + H2O2 = hematinic acid + a tripyrrole + Fe3+
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYSTEMATIC NAME
IUBMB Comments
protoheme,hydrogen peroxide oxidoreductase (porphyrin cleaving)
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
protoporphyrin IX + ascorbate + O2
hematinic acid + a tripyrrole + Fe3+
Substrates: cosubstrate is hydrogen peroxide that is formed in solution in the presence of ascorbate and O2
Products: -
Products: -
?
heme + H2O2
hematinic acid + a tripyrrole + Fe3+
A0A4P8B5R6
Substrates: -
Products: -
Products: -
?
heme + H2O2
hematinic acid + a tripyrrole + Fe3+
-
Substrates: -
Products: -
Products: -
?
additional information
?
-
Substrates: enzyme binds and degrades heme in a reaction that releases carbon monoxide. Initial intermediates of the reaction of ChuS with hydrogen peroxide, i.e. a ferrous keto pi neutral radical and ferric verdoheme, are in common with heme oxygenases, while a further reaction step, involving the cleavage of the porphyrin ring at adjacent meso-carbons, results in the release of hematinic acid, a tripyrrole product and non-heme iron in the ferric oxidation state
Products: -
Products: -
?
additional information
?
-
A0A4P8B5R6
Substrates: enzyme ChuS has a significant affinity under anaerobic conditions for heme and can catalyze a peroxide-dependent heme degradation reaction in the presence of ascorbic acid and molecular oxygen. Under anaerobic conditions heme-loaded ChuS is capable of storing heme as well as delivering heme to ChuW for degradation. ChuS is an effective source of heme or protoporphyrin IX for ChuW under anaerobic conditions. Protoporphyrin IX (PPIX)-loaded ChuS is also a viable way to deliver the porphyrin substrate to ChuW and resulting in turnover
Products: -
Products: -
?
additional information
?
-
-
Substrates: determination of heme degradation through measuring free iron in the media
Products: -
Products: -
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
protoporphyrin IX + ascorbate + O2
hematinic acid + a tripyrrole + Fe3+
Substrates: cosubstrate is hydrogen peroxide that is formed in solution in the presence of ascorbate and O2
Products: -
Products: -
?
heme + H2O2
hematinic acid + a tripyrrole + Fe3+
A0A4P8B5R6
Substrates: -
Products: -
Products: -
?
heme + H2O2
hematinic acid + a tripyrrole + Fe3+
-
Substrates: -
Products: -
Products: -
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ciprofloxacin
-
antibiotic, complete enzyme inhibition after 1 h synergistically with imidazole
neomycin
-
antibiotic, complete enzyme inhibition after 1 h, synergistically with imidazole
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
-
screening for heme oxygenase enzyme among clinical isolates of Escherichia coli isolated from urine samples from patient suffering from several type of urinary tract infections, 85% from total sample carry chuS in genetic marker, and about 50% carry all three genes, chuA, chuS and chuT. These isolates show induction and production of HO-1 enzyme, through detection of beliverdin in chochlate agar and also through estimation free iron spectrophotometrically
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
physiological function
additional information
A0A4P8B5R6
ChuS is essentially a tandem repeat of two ChuX-like domains. But structural alignment of the ChuX dimer on the published ChuS model (PDB ID 4CDP) with heme bound yields an RMSD of 4.8 A, with no equivalent heme-ligating residues seen in ChuX
metabolism
A0A4P8B5R6
enzyme ChuS is involved in the aerobic degradation of heme, the roles of ChuS, ChuX, and their interactions with ChuW during anaerobic heme degradation, mechanism of the anaerobic degradation of heme, detailed overview. ChuS is an effective source of heme or protoporphyrin IX for ChuW under anaerobic conditions
metabolism
-
the three genes chuA, chuS and chuT are related to heme oxygenase production. The main gene associated with production of heme oxygenase (HO) is the (chuS) which is responsible for synthesis of this enzyme with the assistance of (chuT) which is responsible for the transport of iron after heme degradation into the cytoplasm of bacteria
physiological function
-
coculture of ChuS-overexpressing Escherichia coli with bone marrow derived macrophages results in decreased IL-12 p40 and increased IL-10 secretion compared to wild-type or ChuS-deficient Escherichia coli. Mice infected with ChuS-overexpressing Escherichia coli have increased levels of hepatic carbon monoxide and decreased serum IL-12 p40
physiological function
A0A4P8B5R6
ChuS facilitates heme or protoporphyrin IX transfer to ChuW during anaerobic porphyrin degradation. ChuS is an effective source of heme or protoporphyrin IX for ChuW under anaerobic conditions. ChuS may have dual functionality in vivo. Specifically, ChuS serves as a heme oxygenase during aerobic metabolism of heme but functions as a cytoplasmic heme storage protein under anaerobic conditions. Under anaerobic conditions heme-loaded ChuS is capable of storing heme as well as delivering heme to ChuW for degradation. ChuS is an effective source of heme or protoporphyrin IX for ChuW under anaerobic conditions. Protoporphyrin IX (PPIX)-loaded ChuS is also a viable way to deliver the porphyrin substrate to ChuW and resulting in turnover
physiological function
-
enzyme ChuS is a heme oxygenase responsible for heme degradation
physiological function
-
coculture of ChuS-overexpressing Escherichia coli with bone marrow derived macrophages results in decreased IL-12 p40 and increased IL-10 secretion compared to wild-type or ChuS-deficient Escherichia coli. Mice infected with ChuS-overexpressing Escherichia coli have increased levels of hepatic carbon monoxide and decreased serum IL-12 p40
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by ultracentrifugation, affinity chromatography, mixture with substrate heme or protoporphyrin IX (PPIX), and gel filtration
A0A4P8B5R6
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene ChuS, the gene is part of a larger heme uptake and utilization operon common to several enteric pathogens, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3). In addition to ChuW, ChuX, and ChuY, ChuS is also expressed from an adjacent operon under iron-limiting conditions
A0A4P8B5R6
gene hcuS, screening of clinical isolates of Escherichia coli isolated from urine sample by PCR analysis
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
incubation of strain NC101 with an iron chelator results in more than 300fold increase in ChuS mRNA expression
incubation of strain NC101 with an iron chelator results in more than 300fold increase in ChuS mRNA expression
-
incubation of strain NC101 with an iron chelator results in more than 300fold increase in ChuS mRNA expression
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Ouellet, Y.H.; Ndiaye, C.T.; Gagne, S.M.; Sebilo, A.; Suits, M.D.; Jubinville, E.; Jia, Z.; Ivancich, A.; Couture, M.
An alternative reaction for heme degradation catalyzed by the Escherichia coli O157 H7 ChuS protein Release of hematinic acid, tripyrrole and Fe(III)
J. Inorg. Biochem.
154
103-113
2016
Escherichia coli (Q8X5N8)
brenda
Maharshak, N.; Ryu, H.S.; Fan, T.J.; Onyiah, J.C.; Schulz, S.; Otterbein, S.L.; Wong, R.; Hansen, J.J.; Otterbein, L.E.; Carroll, I.M.; Plevy, S.E.
Escherichia coli heme oxygenase modulates host innate immune responses
Microbiol. Immunol.
59
452-465
2015
Escherichia coli, Escherichia coli NC101
brenda
Mathew, L.; Beattie, N.; Pritchett, C.; Lanzilotta, W.
New insight into the mechanism of anaerobic heme degradation
Biochemistry
58
4641-4654
2019
Escherichia coli (A0A4P8B5R6)
brenda
Alkreami, M.; Abd-Razzaq, M.; Alsultani, A.
Screening for heme oxygenase enzyme among clinical isolates of Escherichia coli isolated from urine sample
J. Glob. Pharma Technol.
11
215-219
2019
Escherichia coli
-
brenda
EXTERNAL LINKS (specific for EC-Number 1.14.14.B10)
html completed
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2026.1 (March 2026)
About BRENDA
Social media
Help
Survey
Download
Contribution
Legal
Curated at
Member of
![DSMZ Digital Diversity]()
![Global Core Biodata Resource]()
![ELIXIR Core Data Resource]()
![German Network for Bioinformatics Infrastructure]()
