771:
359:
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201:
317:
Higuchi K, Kanazawa K, Nishizawa NK, Chino M, Mori S (1994). "Purification and characterization of nicotianamine synthase from Fe-deficient barley root".
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S-adenosyl-L-methionine:S-adenosyl-L-methionine:S-adenosyl-Lmethioni ne 3-amino-3-carboxypropyltransferase
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299:, specifically those transferring aryl or alkyl groups other than methyl groups. The
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268:3 S-methyl-5'-thioadenosine + nicotianamine
829:
815:
491:
477:
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360:
346:
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433:Farnesyl-diphosphate farnesyltransferase
766:
18:
295:This enzyme belongs to the family of
7:
787:
785:
261:{\displaystyle \rightleftharpoons }
801:. You can help Knowledge (XXG) by
14:
443:Alkylglycerone phosphate synthase
769:
453:Geranylgeranyltransferase type 1
408:Methionine adenosyltransferase
1:
398:Dimethylallyltranstransferase
853:Enzymes of unknown structure
272:Hence, this enzyme has one
874:
784:
248:3 S-adenosyl-L-methionine
647:Michaelis–Menten kinetics
458:Porphobilinogen deaminase
428:Glutathione S-transferase
286:S-methyl-5'-thioadenosine
167:
539:Diffusion-limited enzyme
418:Dihydropteroate synthase
303:of this enzyme class is
278:S-adenosyl-L-methionine
797:-related article is a
262:
224:nicotianamine synthase
22:nicotianamine synthase
632:Eadie–Hofstee diagram
565:Allosteric regulation
263:
642:Lineweaver–Burk plot
252:
448:Farnesyltransferase
423:Spermidine synthase
413:Riboflavin synthase
601:Enzyme superfamily
534:Enzyme promiscuity
331:10.1007/BF00008059
258:
858:Transferase stubs
810:
809:
757:
756:
466:
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438:Spermine synthase
243:chemical reaction
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115:metabolic pathway
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637:Hanes–Woolf plot
580:Enzyme activator
575:Enzyme inhibitor
549:Enzyme catalysis
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16:Class of enzymes
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665:Oxidoreductases
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627:Enzyme kinetics
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611:List of enzymes
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524:Catalytic triad
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301:systematic name
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589:Classification
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325:(2): 173–179.
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606:Enzyme family
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570:Cooperativity
568:
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529:Oxyanion hole
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290:nicotianamine
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153:Gene Ontology
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91:NiceZyme view
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803:expanding it
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743:Translocases
740:
727:
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688:
678:Transferases
675:
662:
519:Binding site
403:Thiaminase I
369:Transferases
322:
318:
304:
297:transferases
294:
271:
223:
217:
79:BRENDA entry
50:161515-44-2
514:Active site
67:IntEnz view
27:Identifiers
842:Categories
717:Isomerases
691:Hydrolases
558:Regulation
319:Plant Soil
311:References
280:, and two
220:enzymology
136:structures
103:KEGG entry
596:EC number
274:substrate
256:⇌
239:catalyzes
56:Databases
848:EC 2.5.1
620:Kinetics
544:Cofactor
507:Activity
282:products
233:) is an
231:2.5.1.43
207:proteins
195:articles
183:articles
140:RCSB PDB
38:2.5.1.43
776:Biology
730:Ligases
500:Enzymes
162:QuickGO
127:profile
110:MetaCyc
45:CAS no.
795:enzyme
792:EC 2.5
762:Portal
704:Lyases
235:enzyme
190:PubMed
172:Search
158:AmiGO
146:PDBsum
86:ExPASy
74:BRENDA
62:IntEnz
33:EC no.
790:This
656:Types
390:2.5.1
373:alkyl
237:that
122:PRIAM
799:stub
748:list
741:EC7
735:list
728:EC6
722:list
715:EC5
709:list
702:EC4
696:list
689:EC3
683:list
676:EC2
670:list
663:EC1
383:2.5)
377:aryl
375:and
288:and
241:the
222:, a
202:NCBI
143:PDBe
98:KEGG
327:doi
323:165
218:In
178:PMC
134:PDB
844::
381:EC
371::
321:.
307:.
292:.
284:,
276:,
228:EC
160:/
830:e
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329::
226:(
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