ID: | 2.6.1.93 |
---|---|
Description: | Neamine transaminase. |
Alternative Name: |
Glutamate--6'-dehydroparomamine aminotransferase. |
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Note: Use your mouse to drag, rotate, and zoom in and out of the structure. Mouse-over to identify atoms and bonds. Mouse controls documentation.UniProtKB Enzyme Link: | UniProtKB 2.6.1.93 |
BRENDA Enzyme Link: | BRENDA 2.6.1.93 |
KEGG Enzyme Link: | KEGG2.6.1.93 |
BioCyc Enzyme Link: | BioCyc 2.6.1.93 |
ExPASy Enzyme Link: | ExPASy2.6.1.93 |
EC2PDB Enzyme Link: | EC2PDB 2.6.1.93 |
ExplorEnz Enzyme Link: | ExplorEnz 2.6.1.93 |
PRIAM enzyme-specific profiles Link: | PRIAM 2.6.1.93 |
IntEnz Enzyme Link: | IntEnz 2.6.1.93 |
MEDLINE Enzyme Link: | MEDLINE 2.6.1.93 |
RHEA:34039 | 2-oxoglutarate + neamine = 6'-oxoparomamine + L-glutamate |
RULE(radius=1) | [*:1]-[C;H0;+0:2](-[*:3])=[O;H0;+0:4].[*:5]-[CH;+0:6](-[*:7])-[O;H0;+0:8]-[CH;+0:9](-[*:10])-[CH2;+0:11]-[NH2;+0:12]>>[*:1]-[CH;+0:2](-[*:3])-[NH2;+0:12].[*:5]-[CH;+0:6](-[*:7])-[O;H0;+0:4]-[CH;+0:9](-[*:10])-[CH;+0:11]=[O;H0;+0:8] |
Reaction | ![]() |
Core-to-Core | No scaffolds atoms were exchanged as a result of the reaction |
Title | Authors | Date | PubMed ID |
---|---|---|---|
Discovery of parallel pathways of kanamycin biosynthesis allows antibiotic manipulation. | Park JW, Park SR, Nepal KK, Han AR, Ban YH, Yoo YJ, Kim EJ, Kim EM, Kim D, Sohng JK, Yoon YJ | 2011 Oct 9 | 21983602 |
The oxidoreductases LivQ and NeoQ are responsible for the different 6'-modifications in the aminoglycosides lividomycin and neomycin. | Clausnitzer D, Piepersberg W, Wehmeier UF | 2011 Sep | 21689223 |
Elaboration of neosamine rings in the biosynthesis of neomycin and butirosin. | Huang F, Spiteller D, Koorbanally NA, Li Y, Llewellyn NM, Spencer JB | 2007 Feb 12 | 17206729 |