EC number:1.8.4.2

Enzyme

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EC Tree
     1. Oxidoreductases
        1.8 Acting on a sulfur group of donors
            1.8.4 With a disulfide as acceptor
ID:1.8.4.2
Description:Protein-disulfide reductase (glutathione).
Alternative Name: Insulin reductase.
Glutathione--insulin transhydrogenase.
Prosite: PDOC00172;
PDB:
PDBScop
6IBL 8091151; 8091152; 8031981; 8044359; 8091151; 8091152; 8031981; 8044359;
6H7O 8091151; 8091152; 8031981; 8044359; 8091151; 8091152; 8031981; 8044359;
6H7N 8091151; 8091152; 8031981; 8044359; 8091151; 8091152; 8031981; 8044359;
6H7M 8091151; 8091152; 8031981; 8044359; 8091151; 8091152; 8031981; 8044359;
6H7L 8091151; 8091152; 8031981; 8044359; 8091151; 8091152; 8031981; 8044359;
 » show all
Cath: 3.40.30.10;

3D structure

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PDB

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6IBL; 6H7O; 6H7N; 6H7M; 6H7L; 6H7J; 3DXB; 1X5C; 1MEK; 3WT1; 3WT2; 5CRW; 2RUF; 2RUE; 2KP1; 2DJJ; 3UEM; 4EL1; 4EKZ; 1ZOF; 1WE0; 2BMX; 4XTS; 1N8J; 1YF1; 5UKA; 4XS6; 4XS4; 4XS1; 4XRD; 4XRA; 4MAB; 4MA9; 3EMP; 1YF0; 1YEX; 1YEP; 1PSQ; 2A4V; 3A5W; 3A2W; 3A2V; 2ZCT; 2NVL; 2E2M; 2E2G; 2CV4; 1X0R; 5XBS; 5ID2; 1XXU; 5C04; 4XIH; 4X1U; 1XVW; 1TP9; 5B6N; 5B6M; 1PRX; 2Z9S; 1QQ2; 5IJT; 1QMV; 6GXY; 6GXG; 1XZO; 1ON4; 1LU4; 2H1B; 3C73; 2H1G; 2H1D; 2H1A; 2H19; 2F9S; 1SU9; 1ST9; 3C71; 1Y25; 1XVQ; 1Q98; 3HVX; 3I43; 3HVS; 1QXH; 4AF2; 3HVV; 1KNG; 2B1L; 1Z5Y; 3K8N; 2G0F; 2B1K; 1H4O; 4MMM; 2VL9; 4K7O; 4K7N; 4K7I; 2VL3; 2VL2; 1OC3; 3MNG; 1URM; 1HD2; 2B5Y; 2B5X; 4PUF; 4MH3; 4MH2; 1ZYE; 1FB6; 1FB0; 1GL8; 1F9M; 1FAA; 1NW2; 1NSW; 1RQM; 1QUW; 1THX; 5HR1; 2FCH; 1F6M; 2EIR; 2EIO; 1ZCP; 4X43; 6GD1; 5HR3; 5HR0; 4HU7; 3DYR; 2TRX; 2H76; 2H75; 2H74; 2H73; 2H72; 2H71; 2H70; 2H6Z; 2H6Y; 2H6X; 2FD3; 1ZZY; 1KEB; 2O8V; 1X9W; 1X9M; 1TKD; 1SL2; 1SL1; 1SKW; 1SKS; 1SKR; 5HR2; 4HUA; 4HU9; 1XOB; 1XOA; 1TXX; 1THO; 1SRX; 1XWB; 1XWA; 1XW9; 1XWC; 5XOC; 1M7T; 4POM; 4POL; 4POK; 2IFQ; 2HXK; 4OO4; 4LL4; 4LL1; 3QFB; 3M9K; 3M9J; 3E3E; 5DQY; 4TRX; 4OO5; 3TRX; 3KD0; 2IIY; 2HSH; 1TRW; 1TRV; 1TRU; 1TRS; 1MDK; 1MDJ; 1MDI; 1ERW; 1ERV; 1ERU; 1ERT; 1CQH; 1CQG; 1AUC; 1AIU; 1XFL; 1SYR; 4J56; 4J57; 2MMO; 2MMN; 1VRS; 4IP6; 4IP1; 2FWH; 2FWG; 2FWF; 2FWE; 2AJQ; 1SL0; 1ZYQ; 1X9S; 1TK8; 1TK5; 1TK0; 1T8E; 1T7P; 2K8V; 1SEN; 2IPA; 2PVO; 2PUK; 6Q6V; 6Q6U; 6Q47; 6Q46; 6I19; 1EP8; 1EP7; 6Q6T; 1TOF; 1BQ7; 4TKY; 1U3A; 6BR4; 6BQX; 4ZIJ; 2B6M; 2B3S; 1FVK; 1FVJ; 1DSB; 1ACV; 1AC1; 1A2M; 1A2L; 3E9J; 2ZUP; 2LEG; 2NDO; 1UN2; 1TI1; 1A2J; 1A24; 1A23; 4DVC; 2IJY; 1BED; 1EEJ; 1TJD; 3HY2; 2RII; 2HI7; 1GH2; 2BTO; 5IKN; 5E4W; 2K9F; 2JZS; 2JZR; 2FY6; 4TXO; 4TXV; 1JFU; 6ENY; 3BOA; 2B5E; 1NM3; 6NUP; 6MZA; 6IU1; 6IU0; 6ITZ; 6HF1; 6GC1; 6G62; 6G61; 6DNL; 6BKV; 5ZTE; 5YRY; 5YKW; 5YKJ; 5XWM; 5XF7; 5XBR; 5XBQ; 5VO7; 5UCX; 5TLQ; 5OVQ; 5JCG; 5J9C; 5J9B; 5IPH; 5IPG; 5IOX; 5IOW; 5IO2; 5IO0; 5INY; 5IMZ; 5IMV; 5IMF; 5IMD; 5IMC; 5IMA; 5IM9; 5HQP; 5GU7; 5GU6; 5EPT; 5EPF; 5DVB; 5DCH; 5D96; 5D93; 5D8I; 5CYY; 5B8B; 5B8A; 5AYL; 5AYK; 4ZL9; 4ZL8; 4ZL7; 4XCS; 4X0X; 4RQX; 4P2L; 4OWY; 4NMU; 4ILF; 4IJ3; 4I5Q; 4H86; 4GWR; 4EF0; 4DSS; 4DSR; 4DSQ; 3WGX; 3WGE; 3WGD; 3W8J; 3W6G; 3VWW; 3VWV; 3VWU; 3UVT; 3UJ1; 3TKS; 3TKR; 3TKQ; 3TKP; 3TJK; 3TJJ; 3TJG; 3TJF; 3TJB; 3T59; 3T58; 3SBC; 3QOU; 3QFA; 3Q6O; 3PIN; 3O6T; 3L9S; 3KH9; 3KH7; 3IDV; 3HD5; 3H93; 3GKN; 3GKM; 3GKK; 3GHA; 3GH9; 3F8U; 3F3R; 3F3Q; 3EU4; 3EU3; 3ERW; 3ED3; 3DKS; 3DIE; 3D6I; 3D22; 3D21; 3APS; 3APQ; 3APO; 3A2X; 2YZH; 2WZ9; 2VOC; 2TIR; 2R2J; 2PU9; 2PN8; 2OE3; 2OE1; 2OE0; 2O89; 2O87; 2O85; 2O7K; 2N5B; 2N5A; 2MBT; 2L59; 2L4Q; 2JU5; 2JSZ; 2JSY; 2I9H; 2I1U; 2HYX; 2HSY; 2H30; 2GZZ; 2GZY; 2FA4; 2EIQ; 2DMM; 2DML; 2DJ3; 2DJ2; 2DJ1; 2DIZ; 2DIY; 2ALB; 1X5E; 1X5D; 1WMJ; 1W89; 1W4V; 1UVZ; 1UC7; 1T00; 1OAZ; 1O73; 1DBY;

References

External Links

UniProtKB Enzyme Link: UniProtKB 1.8.4.2
BRENDA Enzyme Link: BRENDA 1.8.4.2
KEGG Enzyme Link: KEGG1.8.4.2
BioCyc Enzyme Link: BioCyc 1.8.4.2
ExPASy Enzyme Link: ExPASy1.8.4.2
EC2PDB Enzyme Link: EC2PDB 1.8.4.2
ExplorEnz Enzyme Link: ExplorEnz 1.8.4.2
PRIAM enzyme-specific profiles Link: PRIAM 1.8.4.2
IntEnz Enzyme Link: IntEnz 1.8.4.2
MEDLINE Enzyme Link: MEDLINE 1.8.4.2

EC number:1.8.4.2

MSA:

1.8.4.2;
Phylogenetic Tree:

1.8.4.2;
Uniprot:
M-CSA:
RHEA:21064 [protein]-disulfide + 2 glutathione = [protein]-dithiol + glutathione disulfide
RULE(radius=1) [*:1]-[S;H0;+0:2]-[S;H0;+0:3]-[*:4].[*:5]-[SH;+0:6].[*:7]-[SH;+0:8]>>[*:5]-[S;H0;+0:6]-[S;H0;+0:8]-[*:7].[*:1]-[SH;+0:2].[*:4]-[SH;+0:3]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Di-fluoresceinthiocarbamyl-insulin: a fluorescent substrate for the assay of protein disulfide oxidoreductase activity.Heuck AP, Wolosiuk RA1997 May 159177728
Functional characterization of ERp18, a new endoplasmic reticulum-located thioredoxin superfamily member.Alanen HI, Williamson RA, Howard MJ, Lappi AK, Jäntti HP, Rautio SM, Kellokumpu S, Ruddock LW2003 Aug 112761212
Kinetic analysis of the mechanism of insulin degradation by glutathione-insulin transhydrogenase (thiol: protein-disulfide oxidoreductase).Chandler ML, Varandani PT1975 May 201170876