274:
1065:
308:: A 4 iron-4 sulfur cluster is required for formation of a 5'-deoxyadenosyl radical. This radical then acts as the "stable" radical carrier in the reaction mechanism which transfers the radical to the amino acid.
296:(PLP): Responsible for binding of the amino acid during reaction. The pi-system of this molecule facilitates radical delocalization during formation of an aziridinyl radical. The structure is given below:
346:: The 5'-deoxyadenosyl radical is transferred to the amino acid and an aziridinyl radical is formed. In this configuration, the radical is stabilized by the pi-system of pyridoxal phosphate.
244:
361:
163:
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182:
727:
652:
175:
352:: In the final step, the new amino acid is formed and the radical is returned to its more stable state on the 5'-deoxyadenosyl.
254:
Shown on the right is the three-dimensional structure of the Lysine 2,3-aminomutase protein. The structure was determined by
142:
550:
Bhandari DM, Fedoseyenko D, Begley TP (2018). "Mechanistic
Studies on the Radical SAM Enzyme Tryptophan Lyase (NosL)".
258:
to 2.1 Angstrom resolution and was seen to crystallize as a homotetramer. KAM was first purified and characterized in
784:
626:
567:
488:
Aberhart DJ, Gould SJ, Lin HJ, Thiruvengadam TK, Weiller BH (1981). "Stereochemistry of lysine 2,3-aminomutase".
340:: The amino acid (Lysine or Beta-Lysine depending on forward or reverse reactions) binds to pyridoxal phosphate.
515:
Zappia V, Barker HA (June 1970). "Studies on lysine-2,3-aminomutase. Subunit structure and sulfhydryl groups".
136:
118:
940:
123:
283:
Four key cofactors are required for the reaction catalyzed by the lysine 2,3-aminomutase enzyme. They are:
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1085:
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431:"The x-ray crystal structure of lysine-2,3-aminomutase from Clostridium subterminale"
403:
130:
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873:
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842:
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555:
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239:(SAM) activated radical reaction pathway. The generalized reaction is shown below:
920:
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958:
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435:
Proceedings of the
National Academy of Sciences of the United States of America
398:
382:"Lysine 2,3-aminomutase: is adenosylmethionine a poor man's adenosylcobalamin?"
381:
158:
604:
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863:
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232:
455:
328:
mechanism in which a S-adenosyl methionine forms a 5'-deoxyadenosyl radical.
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290:(SAM): Helps generate the radical intermediate by borrowing an electron.
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1023:
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302:: Required for coordination between the dimers in the protein.
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487:
334:: Lysine 2,3-aminomutase binds to pyridoxal phosphate (PLP).
710:
705:
299:
94:
762:
554:. Methods in Enzymology. Vol. 606. pp. 155–178.
429:
Lepore BW, Ruzicka FJ, Frey PA, Ringe D (September 2005).
549:
356:
The reaction mechanism described above is shown below:
428:
1053:
227:. It accomplishes this interconversion using three
317:The generalized reaction takes place in 5 steps:
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778:
620:
514:
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597:at the U.S. National Library of Medicine
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324:: A "stable" radical is formed through a
272:
216:that facilitates the conversion of the
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200:Lysine 2,3-aminomutase (KAM or LAM)
13:
265:for studies of Lysine metabolism.
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588:
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359:
242:
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508:
481:
1:
529:10.1016/s0005-2795(70)80013-7
517:Biochimica et Biophysica Acta
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268:
249:
7:
792:
10:
1102:
718:Phosphoenolpyruvate mutase
691:Bisphosphoglycerate mutase
560:10.1016/bs.mie.2018.06.008
399:10.1096/fasebj.7.8.8500691
949:
941:Michaelis–Menten kinetics
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667:Precorrin-8X methylmutase
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833:Diffusion-limited enzyme
752:Methylmalonyl-CoA mutase
599:Medical Subject Headings
686:Phosphoglycerate mutase
662:Lysolecithin acylmutase
456:10.1073/pnas.0505726102
595:Lysine+2,3-aminomutase
280:
19:Lysine 2,3-aminomutase
926:Eadie–Hofstee diagram
859:Allosteric regulation
737:Cycloartenol synthase
350:Amino Acid Conversion
288:S-Adenosyl methionine
276:
256:X-ray crystallography
237:S-Adenosyl methionine
936:Lineweaver–Burk plot
380:Frey PA (May 1993).
235:radical formed in a
742:Lanosterol synthase
552:Radical SAM Enzymes
502:10.1021/ja00412a040
447:2005PNAS..10213819L
306:Iron-sulfur cluster
294:Pyridoxal phosphate
278:Pyridoxal phosphate
895:Enzyme superfamily
828:Enzyme promiscuity
701:Phosphomannomutase
696:Phosphoglucomutase
338:Amino Acid Binding
313:Reaction Mechanism
281:
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496:(22): 6750–6752.
322:Radical Formation
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112:metabolic pathway
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931:Hanes–Woolf plot
874:Enzyme activator
869:Enzyme inhibitor
843:Enzyme catalysis
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344:Radical Transfer
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959:Oxidoreductases
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921:Enzyme kinetics
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905:List of enzymes
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818:Catalytic triad
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747:Lupeol synthase
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883:Classification
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679:Phosphomutases
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589:External links
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332:Enzyme Binding
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900:Enzyme family
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864:Cooperativity
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823:Oxyanion hole
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523:(3): 505–13.
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386:FASEB Journal
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233:deoxyadenosyl
230:
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88:NiceZyme view
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1037:Translocases
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1021:
1008:
995:
982:
972:Transferases
969:
956:
813:Binding site
730:Other groups
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263:subterminale
259:
253:
241:
199:
198:
76:BRENDA entry
808:Active site
655:Acyl Groups
326:radical SAM
261:Clostridium
225:beta-lysine
211:radical SAM
64:IntEnz view
24:Identifiers
1011:Isomerases
985:Hydrolases
852:Regulation
367:References
300:Zinc metal
218:amino acid
133:structures
100:KEGG entry
47:9075-20-1
890:EC number
636:Isomerase
269:Cofactors
250:Structure
231:and a 5'-
229:cofactors
53:Databases
1086:EC 5.4.3
1080:Category
914:Kinetics
838:Cofactor
801:Activity
578:30097091
475:16166264
416:33374466
188:proteins
176:articles
164:articles
137:RCSB PDB
1070:Biology
1024:Ligases
794:Enzymes
640:mutases
537:5452674
466:1236562
443:Bibcode
408:8500691
209:) is a
207:5.4.3.2
124:profile
107:MetaCyc
42:CAS no.
35:5.4.3.2
1056:Portal
998:Lyases
728:5.4.99
601:(MeSH)
576:
566:
535:
473:
463:
414:
406:
221:lysine
214:enzyme
171:PubMed
153:Search
143:PDBsum
83:ExPASy
71:BRENDA
59:IntEnz
30:EC no.
950:Types
677:5.4.2
653:5.4.1
412:S2CID
119:PRIAM
1042:list
1035:EC7
1029:list
1022:EC6
1016:list
1009:EC5
1003:list
996:EC4
990:list
983:EC3
977:list
970:EC2
964:list
957:EC1
711:PMM2
706:PMM1
646:5.4)
574:PMID
564:ISBN
533:PMID
471:PMID
404:PMID
183:NCBI
140:PDBe
95:KEGG
556:doi
525:doi
521:207
498:doi
494:103
461:PMC
451:doi
439:102
394:doi
223:to
159:PMC
131:PDB
1082::
644:EC
638::
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562:.
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449:.
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388:.
384:.
204:EC
1058::
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988:(
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962:(
786:e
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642:(
628:e
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396::
390:7
202:(
Text is available under the Creative Commons Attribution-ShareAlike License. Additional terms may apply.