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Information on EC 1.1.1.329 - 2-deoxy-scyllo-inosamine dehydrogenase Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
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The expected taxonomic range for this enzyme is: Streptomyces
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2-deoxy-scyllo-inosamine dehydrogenase
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2-deoxy-scyllo-inosamine + NAD(P)+ = 3-amino-2,3-dideoxy-scyllo-inosose + NAD(P)H + H+
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Biosynthesis of antibiotics
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kanamycin biosynthesis
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Neomycin, kanamycin and gentamicin biosynthesis
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paromamine biosynthesis I
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2-deoxy-scyllo-inosamine:NAD(P)+ 1-oxidoreductase
Requires zinc. Involved in the biosynthetic pathways of several clinically important aminocyclitol antibiotics, including kanamycin, neomycin and ribostamycin. cf. EC 1.1.99.38, 2-deoxy-scyllo-inosamine dehydrogenase (AdoMet-dependent).
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kanK
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gene name
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neoA
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gene name
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UniProt
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UniProt
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UniProt
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UniProt
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physiological function
heterologous expression of enzyme in combination with Streptomyces kanamyceticus genes kacA, KanF, and kanAB in Streptomyces lividans leads to production of paromamine, an intermediate in kanamycin biosynthesis
physiological function
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heterologous expression of enzyme in combination with Streptomyces kanamyceticus genes kacA, KanF, and kanAB in Streptomyces lividans leads to production of paromamine, an intermediate in kanamycin biosynthesis
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2-deoxy-scyllo-inosamine + NAD+
3-amino-2,3-dideoxy-scyllo-inosose + NADH + H+
2-deoxy-scyllo-inosamine + NADP+
3-amino-2,3-dideoxy-scyllo-inosose + NADPH + H+
2-deoxy-scyllo-inosamine + NAD+
3-amino-2,3-dideoxy-scyllo-inosose + NADH + H+
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2-deoxy-scyllo-inosamine + NAD+
3-amino-2,3-dideoxy-scyllo-inosose + NADH + H+
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2-deoxy-scyllo-inosamine + NADP+
3-amino-2,3-dideoxy-scyllo-inosose + NADPH + H+
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2-deoxy-scyllo-inosamine + NADP+
3-amino-2,3-dideoxy-scyllo-inosose + NADPH + H+
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NAD+
enzyme accepts both NAD+ and NADP+
NADP+
enzyme accepts both NAD+ and NADP+
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Zn2+
assay in presence of
Zn2+
presence of Zn2+. The two zinc coordination motifs associated with catalytic and structural zinc ions are important for the construction of the active site and are highly conserved in this family
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expression in Escherichia coli
expression in Streptomyces lividans
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DOIAD_STRSD
Streptoalloteichus tenebrarius (strain ATCC 17920 / DSM 40477 / NCIB 11028)
339
35377
Swiss-Prot
DOIAD_STRKN
343
35936
Swiss-Prot
DOIAD_STRRI
340
35413
Swiss-Prot
DOIAD_STRRY
339
35458
Swiss-Prot
DOIAD_MICEC
340
36023
Swiss-Prot
DOIAD_STRLV
339
35290
Swiss-Prot
DOIAD_STRFR
340
35228
Swiss-Prot
A0A0W1KKB1_9ACTO
347
36660
TrEMBL
A0A1J5QB93_9ZZZZ
339
35905
TrEMBL
A0A1E3H3R0_9RHIZ
326
34190
TrEMBL
A0A1E3AZJ7_9FIRM
311
34011
TrEMBL
A0A100JAV3_9ACTN
335
34981
TrEMBL
A0A0M2H7M5_9MICO
335
34989
TrEMBL
A0A1E7XGI3_9LACO
333
35920
TrEMBL
A0A1D2I844_9ACTN
345
35656
TrEMBL
A0A143PIC1_9BACT
347
36321
TrEMBL
A0A0M2H0J1_9MICO
337
35035
TrEMBL
A0A0U5M5P3_STRRE
326
33737
TrEMBL
A0A0J5PDG6_9LACT
338
36269
TrEMBL
A0A1E3A8P9_9FIRM
311
34102
TrEMBL
A0A1D7ZWZ4_LACFE
356
38385
TrEMBL
A0A150HD29_9MICO
343
37250
TrEMBL
A0A0D1LY90_9LACT
338
36066
TrEMBL
A0A100JSL4_STRSC
346
35714
TrEMBL
A0A0J6ZIQ6_9MYCO
322
34617
TrEMBL
A0A1D8G9V9_9ACTN
340
35228
TrEMBL
A0A0L0JW88_9ACTN
334
34909
TrEMBL
A0A1J5QRB4_9ZZZZ
322
33431
TrEMBL
A0A177HGA3_9ACTN
336
34793
TrEMBL
A0A0J6W9Z5_9MYCO
322
34685
TrEMBL
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Kudo, F.; Yamamoto, Y.; Yokoyama, K.; Eguchi, T.; Kakinuma, K.
Biosynthesis of 2-deoxystreptamine by three crucial enzymes in Streptomyces fradiae NBRC 12773
J. Antibiot.
58
766-774
2005
Streptomyces fradiae (Q53U21), Streptomyces fradiae, Streptomyces fradiae NBRC 12773 (Q53U21)
brenda
Nepal, K.; Oh, T.; Sohng, J.
Heterologous production of paromamine in Streptomyces lividans TK24 using kanamycin biosynthetic genes from Streptomyces kanamyceticus ATCC12853
Mol. Cells
27
601-608
2009
Streptomyces kanamyceticus (Q6L743), Streptomyces kanamyceticus ATCC12853 (Q6L743)
brenda
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