Information on EC 5.4.4.1 -

Information on EC 5.4.4.1 - (hydroxyamino)benzene mutase:

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EC NUMBER	COMMENTARY
5.4.4.1	-

RECOMMENDED NAME	GeneOntology No.
(hydroxyamino)benzene mutase	GO:0018824

REACTION	REACTION DIAGRAM	COMMENTARY	ORGANISM	UNIPROT ACCESSION NO.	LITERATURE
(hydroxyamino)benzene = 2-aminophenol		-	-	-	-
(hydroxyamino)benzene = 2-aminophenol		intramolecular hydroxyl transfer	Pseudomonas pseudoalcaligenes	-	639029
(hydroxyamino)benzene = 2-aminophenol		intramolecular hydroxyl transfer; proposed intramolecular rearrangment mechanism, different from the nonenzymatic Bamberger reaction which proceeds via intermolecular hydroxyl transfer	Pseudomonas pseudoalcaligenes	-	639030

REACTION TYPE	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
dismutation	-	-	-	-

PATHWAY	KEGG Link	MetaCyc Link
nitrobenzene degradation I	-	PWY-5637

SYSTEMATIC NAME	IUBMB Comments
(hydroxyamino)benzene hydroxymutase	-

SYNONYMS	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
CnbB	Comamonas sp.	-	-	677659
HAB mutase	-	-	-	-
hydroxylaminobenzene hydroxymutase	-	-	-	-
hydroxylaminobenzene mutase	-	-	-	-

CAS REGISTRY NUMBER	COMMENTARY
261765-91-7	-

ORGANISM	COMMENTARY	LITERATURE	SEQUENCE CODE	SEQUENCE DB	SOURCE
Comamonas sp.	strain CNB-1 able to grow on 4-chloronitrobenzene and nitrobenzene as sole carbon sources. Enzymes involved in 4-chloronitrobenzene and nitrobenzene degradation are chloronitrobenzene nitroreductase, hydroxylaminobenzene mutase, 2-aminophenol 1,6-dioxygenase, and 2-aminomuconic semialdehyde dehydrogenase. When these enzymes are coupled in vitro, they sequentially catalyze the conversions of 4-chloronitrobenzene to 2-amino-5-chloromuconic acid and nitrobenzene to 2-aminomuconic acid	677659	-	-
Comamonas sp. CNB-1	strain CNB-1 able to grow on 4-chloronitrobenzene and nitrobenzene as sole carbon sources. Enzymes involved in 4-chloronitrobenzene and nitrobenzene degradation are chloronitrobenzene nitroreductase, hydroxylaminobenzene mutase, 2-aminophenol 1,6-dioxygenase, and 2-aminomuconic semialdehyde dehydrogenase. When these enzymes are coupled in vitro, they sequentially catalyze the conversions of 4-chloronitrobenzene to 2-amino-5-chloromuconic acid and nitrobenzene to 2-aminomuconic acid	677659	-	-
Pseudomonas pseudoalcaligenes	-	639029, 639030	-	-
Pseudomonas pseudoalcaligenes	encoded on 2 genes, habA and habB, only habA is expressed; strain JS45	639028	-	-
Pseudomonas pseudoalcaligenes	expression in Escherichia coli, together with nitrobenzene nitroreductase	660747	-	-
Pseudomonas pseudoalcaligenes	strain JS45	639027	-	-
Pseudomonas putida	strain ZWL73	677735	-	-
Pseudomonas putida ZWL73	strain ZWL73	677735	-	-

GENERAL INFORMATION	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
No entries in this field

SUBSTRATE	PRODUCT	REACTION DIAGRAM	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY/ Substrate	LITERATURE/ Substrate	COMMENTARY/ Product	LITERATURE/ Product	Reversibility r=reversible ir=irreversible ?=not specified
(hydroxyamino)benzene	2-aminophenol		Pseudomonas pseudoalcaligenes	-	-	639029	-	-	-
(hydroxyamino)benzene	2-aminophenol		Pseudomonas pseudoalcaligenes	-	highly selective for the production of the ortho-isomer	639028	highly selective for the production of the ortho-isomer	639028	-
(hydroxyamino)benzene	2-aminophenol		Pseudomonas pseudoalcaligenes	-	highly selective for the production of the ortho-isomer	639027	highly selective for the production of the ortho-isomer	639027	?
4-chloro-(hydroxyamino)benzene	2-amino-5-chlorophenol		Pseudomonas putida	-	in presence of chloronitrobenzene nitroreductase, degradation of 4-chloronitrobenzene to 2-amino-5-chlorophenol, which is the ring-cleavage substrate in degradation of 4-chloronitrobenzene	677735	-	-	?
4-hydoxyaminobiphenyl ether	2-amino-5-phenoxyphenol		Pseudomonas pseudoalcaligenes	-	-	639027	-	639027	?
4-hydroxyylaminobenzoate	4-amino-3-hydroxybenzoate		Pseudomonas pseudoalcaligenes	-	-	639030	-	639030	?
additional information	?	-	Comamonas sp.	-	enzymes involved in 4-chloronitrobenzene and nitrobenzene degradation are chloronitrobenzene nitroreductase, hydroxylaminobenzene mutase, 2-aminophenol 1,6-dioxygenase, and 2-aminomuconic semialdehyde dehydrogenase. When these enzymes are coupled in vitro, they sequentially catalyze the conversions of 4-chloronitrobenzene to 2-amino-5-chloromuconic acid and nitrobenzene to 2-aminomuconic acid	677659	-	-	-

NATURAL SUBSTRATES	NATURAL PRODUCTS	REACTION DIAGRAM	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY SUBSTRATE	LITERATURE (Substrate)	COMMENTARY PRODUCT	LITERATURE (Product)
No entries in this field

COFACTOR	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE	IMAGE
No entries in this field

METALS and IONS	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
No entries in this field

INHIBITORS	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE	IMAGE
Triton X-100	Pseudomonas pseudoalcaligenes	-	0.5%	639029	2D-image
Zn2+	Pseudomonas pseudoalcaligenes	-	1 mM, 70% inhibition	639029	2D-image

ACTIVATING COMPOUND	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE	IMAGE
No entries in this field

KM VALUE [mM]	KM VALUE [mM] Maximum	SUBSTRATE	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE	IMAGE
0.15	-	(hydroxylamino)benzene	Pseudomonas pseudoalcaligenes	-	at pH 7.0	639029	2D-image

TURNOVER NUMBER [1/s]	TURNOVER NUMBER MAXIMUM[1/s]	SUBSTRATE	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE	IMAGE
No entries in this field

kcat/KM VALUE [1/mMs^-1]	kcat/KM VALUE [1/mMs^-1] Maximum	SUBSTRATE	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE	IMAGE
No entries in this field

Ki VALUE [mM]	Ki VALUE [mM] Maximum	INHIBITOR	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE	IMAGE
No entries in this field

IC50 VALUE [mM]	IC50 VALUE [mM] Maximum	INHIBITOR	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE	IMAGE
No entries in this field

SPECIFIC ACTIVITY [µmol/min/mg]	SPECIFIC ACTIVITY MAXIMUM	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
38	-	Pseudomonas pseudoalcaligenes	-	-	639029

pH OPTIMUM	pH MAXIMUM	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
No entries in this field

pH RANGE	pH RANGE MAXIMUM	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
6.5	9.5	Pseudomonas pseudoalcaligenes	-	56% and 59% of maximal activity at pH 6.5 and pH 9.5 respectively	639029

TEMPERATURE OPTIMUM	TEMPERATURE OPTIMUM MAXIMUM	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
No entries in this field

TEMPERATURE RANGE	TEMPERATURE MAXIMUM	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
No entries in this field

pI VALUE	pI VALUE MAXIMUM	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
No entries in this field

SOURCE TISSUE	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE	SOURCE
No entries in this field

LOCALIZATION	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	GeneOntology No.	LITERATURE	SOURCE
additional information	Pseudomonas pseudoalcaligenes	-	not an integral membrane protein	-	639028

PDB	SCOP	CATH	ORGANISM
No entries in this field

MOLECULAR WEIGHT	MOLECULAR WEIGHT MAXIMUM	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
additional information	-	Pseudomonas pseudoalcaligenes	-	mutase forms high-molecular-mass complexes which elute with the void-volume, mutase tends to associate even in the presence of SDS	639029

SUBUNITS	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
?	Comamonas sp.	-	x * 15951, calculated	677659

POSTTRANSLATIONAL MODIFICATION	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
No entries in this field

Crystallization/COMMENTARY	ORGANISM	UNIPROT ACCESSION NO.	LITERATURE
No entries in this field

pH STABILITY	pH STABILITY MAXIMUM	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
No entries in this field

TEMPERATURE STABILITY	TEMPERATURE STABILITY MAXIMUM	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
60	-	Pseudomonas pseudoalcaligenes	-	recombinant HabA, inactivation above, 50% loss of activity at 70�C after 10 min	639028
85	-	Pseudomonas pseudoalcaligenes	-	recombinant HabB, no loss of activity after 10 min	639028

GENERAL STABILITY	ORGANISM	UNIPROT ACCESSION NO.	LITERATURE
mutase in crude extracts is stable in the presence of 2% SDS, the partially purified enzyme loses 50% activity in the presence of 0.1% SDS after 30 sec	Pseudomonas pseudoalcaligenes	-	639029

ORGANIC SOLVENT	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
No entries in this field

OXIDATION STABILITY	ORGANISM	UNIPROT ACCESSION NO.	LITERATURE
No entries in this field

STORAGE STABILITY	ORGANISM	UNIPROT ACCESSION NO.	LITERATURE
No entries in this field

Purification/COMMENTARY	ORGANISM	UNIPROT ACCESSION NO.	LITERATURE
Hitrap-SP/Hitrap-Q, filtration/precipitation, Cu2+-chelating chromatography	Pseudomonas pseudoalcaligenes	-	639029
recombinant enzyme	Pseudomonas pseudoalcaligenes	-	639027
recombinant HabB and HabA	Pseudomonas pseudoalcaligenes	-	639028

Cloned/COMMENTARY	ORGANISM	UNIPROT ACCESSION NO.	LITERATURE
expression in Escherichia coli	Comamonas sp.	-	677659
expression of habA and habB in Escherichia coli	Pseudomonas pseudoalcaligenes	-	639028
expression of HabB mutase in Escherichia coli	Pseudomonas pseudoalcaligenes	-	639027
expression in Escherichia coli	Pseudomonas putida	-	677735

EXPRESSION	ORGANISM	UNIPROT ACCESSION NO.	LITERATURE
No entries in this field

ENGINEERING	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
No entries in this field

Renatured/COMMENTARY	ORGANISM	UNIPROT ACCESSION NO.	LITERATURE
No entries in this field

APPLICATION	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
synthesis	Pseudomonas pseudoalcaligenes	-	expression of enzyme plus nitrobenzene nitroreductase in Escherichia coli. Rapid and stoichiometric conversion of nitrobenzene to 2-aminophenol, of 2-nitroacetophenone to 2-amino-3-hydroxyacetophenone, and of 3-nitroacetophenone to 3-amino-2-hydroxyacetophenone, as well as further conversions. Final yields of aminophenols after extraction and recovery are over 64%	660747

REF.	AUTHORS	TITLE	JOURNAL	VOL.	PAGES	YEAR	ORGANISM	LINK TO PUBMED	SOURCE
639027	Nadeau, L.J.; He, Z.; Spain, J.C.	Production of 2-amino-5-phenoxyphenol from 4-nitrobiphenyl ether using nitrobenzene nitroreductase and hydroxylaminobenzene mutase from Pseudomonas pseudoalcaligenes JS45	J. Ind. Microbiol. Biotechnol.	24	301-305	2000	Pseudomonas pseudoalcaligenes	-
639028	Davis, J.K.; Paoli, G.C.; He, Z.; Nadeau, L.J.; Somerville, C.C.; Spain, J.C.	Sequence analysis and initial characterization of two isozymes of hydroxylaminobenzene mutase from Pseudomonas pseudoalcaligenes JS45	Appl. Environ. Microbiol.	66	2965-2971	2000	Pseudomonas pseudoalcaligenes	PubMed
639029	He, Z.; Nadeau, L.J.; Spain, J.C.	Characterization of hydroxylaminobenzene mutase from pNBZ139 cloned from Pseudomonas pseudoalcaligenes JS45: a highly associated SDS-stable enzyme catalyzing an intramolecular transfer of hydroxy groups	Eur. J. Biochem.	267	1110-1116	2000	Pseudomonas pseudoalcaligenes	PubMed
639030	Nadeau, L.J.; He, Z.; Spain, J.C.	Bacterial conversion of hydroxylamino aromatic compounds by both lyase and mutase enzymes involves intramolecular transfer of hydroxyl groups	Appl. Environ. Microbiol.	69	2786-2793	2003	Pseudomonas pseudoalcaligenes	PubMed
660747	Kadiyala, V.; Nadeau, L.J.; Spain, J.C.	Construction of Escherichia coli strains for conversion of nitroacetophenones to ortho-aminophenols	Appl. Environ. Microbiol.	69	6520-6526	2003	Pseudomonas pseudoalcaligenes	PubMed
677659	Wu, J.F.; Jiang, C.Y.; Wang, B.J.; Ma, Y.F.; Liu, Z.P.; Liu, S.J.	Novel partial reductive pathway for 4-chloronitrobenzene and nitrobenzene degradation in Comamonas sp. strain CNB-1	Appl. Environ. Microbiol.	72	1759-1765	2006	Comamonas sp.	PubMed
677735	Xiao, Y.; Wu, J.F.; Liu, H.; Wang, S.J.; Liu, S.J.; Zhou, N.Y.	Characterization of genes involved in the initial reactions of 4-chloronitrobenzene degradation in Pseudomonas putida ZWL73	Appl. Microbiol. Biotechnol.	73	166-171	2006	Pseudomonas putida	PubMed

LINKS TO OTHER DATABASES (specific for EC-Number 5.4.4.1)

NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM

IUBMB Enzyme Nomenclature

PROSITE Database of protein families and domains

Protein Mutant Database

InterPro (database of protein families, domains and functional sites)