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Information on EC 1.17.1.4 - xanthine dehydrogenase and Organism(s) Pseudomonas aeruginosa

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EC Tree
     1 Oxidoreductases
         1.17 Acting on CH or CH2 groups
             1.17.1 With NAD+ or NADP+ as acceptor
                1.17.1.4 xanthine dehydrogenase
IUBMB Comments
Acts on a variety of purines and aldehydes, including hypoxanthine. The mammalian enzyme can also convert all-trans retinol to all-trans-retinoate, while the substrate is bound to a retinoid-binding protein . The enzyme from eukaryotes contains [2Fe-2S], FAD and a molybdenum centre. The mammalian enzyme predominantly exists as the NAD-dependent dehydrogenase (EC 1.17.1.4). During purification the enzyme is largely converted to an O2-dependent form, xanthine oxidase (EC 1.17.3.2). The conversion can be triggered by several mechanisms, including the oxidation of cysteine thiols to form disulfide bonds [2,6,8,15] [which can be catalysed by EC 1.8.4.7, enzyme-thiol transhydrogenase (glutathione-disulfide) in the presence of glutathione disulfide] or limited proteolysis, which results in irreversible conversion. The conversion can also occur in vivo [2,7,15].
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Word Map
The taxonomic range for the selected organisms is: Pseudomonas aeruginosa
The enzyme appears in selected viruses and cellular organisms
Synonyms
xdh/xo, xanthine dehydrogenase/oxidase, atxdh1, paoabc, xanthine:nad+ oxidoreductase, xanthine-nad oxidoreductase, xanthine/nad+ oxidoreductase, xanthine dehydrogenase-1, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
NAD-xanthine dehydrogenase
-
-
-
-
Rosy locus protein
-
-
-
-
xanthine oxidoreductase
-
-
-
-
xanthine-NAD oxidoreductase
-
-
-
-
xanthine/NAD+ oxidoreductase
-
-
-
-
XDH/XO
-
-
-
-
XOR
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -, -, -, -, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
xanthine:NAD+ oxidoreductase
Acts on a variety of purines and aldehydes, including hypoxanthine. The mammalian enzyme can also convert all-trans retinol to all-trans-retinoate, while the substrate is bound to a retinoid-binding protein [14]. The enzyme from eukaryotes contains [2Fe-2S], FAD and a molybdenum centre. The mammalian enzyme predominantly exists as the NAD-dependent dehydrogenase (EC 1.17.1.4). During purification the enzyme is largely converted to an O2-dependent form, xanthine oxidase (EC 1.17.3.2). The conversion can be triggered by several mechanisms, including the oxidation of cysteine thiols to form disulfide bonds [2,6,8,15] [which can be catalysed by EC 1.8.4.7, enzyme-thiol transhydrogenase (glutathione-disulfide) in the presence of glutathione disulfide] or limited proteolysis, which results in irreversible conversion. The conversion can also occur in vivo [2,7,15].
CAS REGISTRY NUMBER
COMMENTARY hide
9054-84-6
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
molybdenum cofactor
-
the enzyme contains molybdenum cofactor comprising only molybdopterin and molybdenum
molybdopterin
-
enzyme contains molybdopterin
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Molybdenum
-
the enzyme contains molybdenum cofactor comprising only molybdopterin and molybdenum
molybdopterin
-
enzyme contains molybdopterin
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
ATCC strain 15692
-
-
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
A0A8G3PC05_PSEAI
484
0
52950
TrEMBL
-
A0A8G3ED70_PSEAI
799
0
87665
TrEMBL
-
A0A8G3K4X6_PSEAI
484
0
52942
TrEMBL
-
A0A509JC00_PSEAI
484
0
52940
TrEMBL
-
A0A8B5B182_PSEAI
484
0
52970
TrEMBL
-
A0A0F6UEY2_PSEAI
799
0
87619
TrEMBL
-
A0A2R3IV66_PSEAI
484
0
52819
TrEMBL
-
A0A6A2K188_PSEAI
799
0
87636
TrEMBL
-
A0A8B4ZYZ4_PSEAI
484
0
52940
TrEMBL
-
A0A8G5D653_PSEAI
799
0
87620
TrEMBL
-
A0A8G7CGR8_PSEAI
799
0
87679
TrEMBL
-
A0A2R3IP96_PSEAI
799
0
87645
TrEMBL
-
A0A8G2Z9X8_PSEAI
799
0
87752
TrEMBL
-
A0A8G2THS0_PSEAI
799
0
87647
TrEMBL
-
A0A8G3WD94_PSEAI
484
0
52970
TrEMBL
-
Q6ZXM3_PSEAI
110
0
12082
TrEMBL
-
A0A8G5Z545_PSEAI
799
0
87757
TrEMBL
-
A0A8G4E6Y0_PSEAI
799
0
87703
TrEMBL
-
Q6ZXL7_PSEAI
110
0
12104
TrEMBL
-
A0A659BFX4_PSEAI
799
0
87683
TrEMBL
-
A0A8G2S064_PSEAI
799
0
87652
TrEMBL
-
A0A8G5LDZ3_PSEAI
484
0
52952
TrEMBL
-
A0A6A9K0D9_PSEAI
484
0
52910
TrEMBL
-
A0A6H3GFV3_PSEAI
799
0
87634
TrEMBL
-
A0A8G8GZ70_PSEAI
484
0
52910
TrEMBL
-
A0A8G6MAP4_PSEAI
799
0
87609
TrEMBL
-
A0A8F9KD43_PSEAI
799
0
87693
TrEMBL
-
A0A241XF80_PSEAI
799
0
87677
TrEMBL
-
A0A8F9JGQ3_PSEAI
799
0
87635
TrEMBL
-
A0A8G4HJY7_PSEAI
484
0
52956
TrEMBL
-
A0A8G6IN47_PSEAI
484
0
52942
TrEMBL
-
A0A8G4MK88_PSEAI
484
0
52968
TrEMBL
-
A0A8G2QL34_PSEAI
484
0
52884
TrEMBL
-
A0A8G4BHB3_PSEAI
799
0
87621
TrEMBL
-
A0A8G3P3N9_PSEAI
484
0
52934
TrEMBL
-
A0A8G7FJJ3_PSEAI
799
0
87621
TrEMBL
-
A0A8G4E2F4_PSEAI
484
0
52956
TrEMBL
-
A0A8G7ATI9_PSEAI
799
0
87694
TrEMBL
-
A0A8G5SA86_PSEAI
484
0
52942
TrEMBL
-
A0A6B1YNU3_PSEAI
484
0
52968
TrEMBL
-
A0A8G2QLL7_PSEAI
799
0
87663
TrEMBL
-
A0A8G7HT86_PSEAI
484
0
52900
TrEMBL
-
A0A643EHJ5_PSEAI
799
0
87626
TrEMBL
-
A0A8G5QN43_PSEAI
484
0
52863
TrEMBL
-
A0A659BKW0_PSEAI
484
0
52882
TrEMBL
-
A0A8G7BR30_PSEAI
484
0
52847
TrEMBL
-
A0A8G2RXN1_PSEAI
484
0
52838
TrEMBL
-
A0A6A9JXA1_PSEAI
799
0
87707
TrEMBL
-
A0A8G7LSA1_PSEAI
799
0
87653
TrEMBL
-
A0A367MFP4_PSEAI
799
0
87664
TrEMBL
-
A0A367MEV3_PSEAI
484
0
52898
TrEMBL
-
A0A8G3ENN5_PSEAI
484
0
52940
TrEMBL
-
A0A8G7IDT1_PSEAI
799
0
87627
TrEMBL
-
A0A8G3YWQ6_PSEAI
799
0
87649
TrEMBL
-
A0A8G4NPX8_PSEAI
799
0
87688
TrEMBL
-
A0A8G6V4E3_PSEAI
799
0
87641
TrEMBL
-
A0A8G4LQG8_PSEAI
484
0
52942
TrEMBL
-
A0A8G4RLS1_PSEAI
799
0
87601
TrEMBL
-
A0A8G4FQU9_PSEAI
484
0
52950
TrEMBL
-
A0A8G4N618_PSEAI
484
0
52859
TrEMBL
-
A0A8F9P1F7_PSEAI
799
0
87677
TrEMBL
-
A0A8G1NLA8_PSEAI
799
0
87636
TrEMBL
-
A0A8G7HZU0_PSEAI
799
0
87667
TrEMBL
-
A0A8G2KPE8_PSEAI
799
0
87731
TrEMBL
-
A0A8G2THQ8_PSEAI
484
0
52968
TrEMBL
-
A0A232DPK5_PSEAI
799
0
87636
TrEMBL
-
Q6ZXM4_PSEAI
110
0
12054
TrEMBL
-
A0A5E5QVC6_PSEAI
799
0
87621
TrEMBL
-
A0A8G7HSD9_PSEAI
799
0
87665
TrEMBL
-
A0A8G4MG37_PSEAI
799
0
87622
TrEMBL
-
A0A0A8RRF8_PSEAI
329
0
35720
TrEMBL
-
A0A069Q2H3_PSEAI
484
0
52912
TrEMBL
-
A0A8F9JY38_PSEAI
484
0
52942
TrEMBL
-
A0A8B4ZBV2_PSEAI
799
0
87649
TrEMBL
-
A0A8B5BIX5_PSEAI
799
0
87649
TrEMBL
-
A0A080VNN2_PSEAI
799
0
87635
TrEMBL
-
A0A8G2KAM3_PSEAI
484
0
52868
TrEMBL
-
A0A643IWY7_PSEAI
484
0
52926
TrEMBL
-
A0A8G6WTY4_PSEAI
484
0
52893
TrEMBL
-
A0A8G6CY41_PSEAI
799
0
87666
TrEMBL
-
A0A8G4L7Y3_PSEAI
799
0
87619
TrEMBL
-
A0A8G3Q5D2_PSEAI
799
0
87608
TrEMBL
-
A0A8G6U4N1_PSEAI
484
0
52896
TrEMBL
-
A0A5K1SGJ0_PSEAI
799
0
87650
TrEMBL
-
A0A8G2KX96_PSEAI
799
0
87649
TrEMBL
-
A0A8G4A3Z3_PSEAI
799
0
87649
TrEMBL
-
A0A8G6WW22_PSEAI
799
0
87789
TrEMBL
-
A0A8G1QBR8_PSEAI
799
0
87652
TrEMBL
-
A0A8G4HJI5_PSEAI
799
0
87637
TrEMBL
-
A0A431XED6_PSEAI
799
0
87636
TrEMBL
-
A0A643IPY0_PSEAI
799
0
87638
TrEMBL
-
Q6ZXM6_PSEAI
110
0
12055
TrEMBL
-
A0A8G7A5T2_PSEAI
484
0
52926
TrEMBL
-
A0A8F9LCG0_PSEAI
484
0
52954
TrEMBL
-
A0A8G3MQR7_PSEAI
799
0
87665
TrEMBL
-
A0A140SIT4_PSEAI
799
0
87666
TrEMBL
-
A0A8G3YK66_PSEAI
799
0
87649
TrEMBL
-
A0A8G7Q255_PSEAI
799
0
87653
TrEMBL
-
A0A8G4YRQ9_PSEAI
799
0
87663
TrEMBL
-
A0A8G5NMX6_PSEAI
799
0
87699
TrEMBL
-
A0A8G5RAS1_PSEAI
484
0
52835
TrEMBL
-
A0A8B5AWR8_PSEAI
799
0
87622
TrEMBL
-
A0A8G4DTH4_PSEAI
484
0
52910
TrEMBL
-
A0A8G3JNM9_PSEAI
484
0
52984
TrEMBL
-
A0A8G5QEE1_PSEAI
799
0
87761
TrEMBL
-
A0A6M3V1P8_PSEAI
484
0
52910
TrEMBL
-
A0A8G7NCU9_PSEAI
799
0
87665
TrEMBL
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Joshi, M.S.; Rajagopalan, K.V.
Specific incorporation of molybdopterin in xanthine dehydrogenase of Pseudomonas aeruginosa
Arch. Biochem. Biophys.
308
331-334
1994
Pseudomonas aeruginosa
Manually annotated by BRENDA team
Johnson, J.L.; Chaudhury, M.; Rajagopalan, K.V.
Identification of a molybdopterin-containing molybdenum cofactor in xanthine dehydrogenase from Pseudomonas aeruginosa
BioFactors
3
103-107
1991
Pseudomonas aeruginosa
Manually annotated by BRENDA team