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arg aminomutase |
Activity |
arg_aminomutase |
Description |
Arginine 2,3-aminomutase (5.4.3.-) |
Notes |
Arginine-2,3-aminomutase should require a [4Fe-4S] cluster, S-adenosyl-L-methionine (SAM), and pyridoxal-5'-phosphate as cofactors.
The sequence in this family are most similar to L-Lysine aminomutases (5.4.3.2); the prototype enzyme (from S. griseochromogenes) is also substantially active towards L-lysine. |
PLP Fold Type |
VII |
PLP-dependent Domain |
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Number of sequences |
10 |
Sequences in seed alignment |
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Reference sequence |
AAP03121 |
Domain interval |
128-289 |
Catalytic site |
348 K |
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References |
Zhao J, Ji W, Ji X, Zhang Q (2020) Biochemical Characterization of an Arginine 2,3‐aminomutase with Dual Substrate Specificity Chin. J. Chem. 38 in press. Cone MC, Yin X, Grochowski LL, Parker MR, Zabriskie TM. (2003) The blasticidin S biosynthesis gene cluster from Streptomyces griseochromogenes: sequence analysis, organization, and initial characterization Chembiochem 4 821-8. Prabhakaran P. C., Woo N-T., Yorgey P.S., Gould S.J. (1988) Biosynthesis of blasticidin S from L-alpha-arginine.
Stereochemistry in the arginine-2,3-aminomutase reaction J. Am. Chem. Soc. 110 5785-91. Articles on arg.aminomutase |
last changed |
2020/04/23 09:13 |
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