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Literature summary extracted from

  • Liu, S.P.; Liu, R.X.; El-Rotail, A.A.; Ding, Z.Y.; Gu, Z.H.; Zhang, L.; Shi, G.Y.
    Heterologous pathway for the production of L-phenylglycine from glucose by E. coli (2014), J. Biotechnol., 186, 91-97.
    View publication on PubMed

Application

EC Number Application Comment Organism
2.6.1.B17 synthesis engineering of Escherichia coli for biosynthesis of L-phenylglycine from glucose. The enzymes HmaS (L-4-hydroxymandelate synthase), Hmo (L-4-hydroxymandelate oxidase) and HpgT (L-4-hydroxyphenylglycine transaminase) are heterologously expressed in Escherichia coli. HpgT conversing phenylglyoxylate to L-phenylglycine uses an unusual aminodonor L-phenylalanine, which releases another phenylpyruvate as the substrate of HmaS. A recycle-reaction maximizes the utilization of precursor phenylpyruvate. After deletionof tyrB and aspC, L-phenylglycine yield increases by 12.6fold. The L-phenylglycine yield is further improved by 14.9fold after enhancing hmaS expression Amycolatopsis orientalis

Organism

EC Number Organism UniProt Comment Textmining
2.6.1.B17 Amycolatopsis orientalis O52815 cf. EC 2.6.1.103
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Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.6.1.B17 phenylglyoxylate + L-phenylalanine
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Amycolatopsis orientalis L-phenylglycine + phenylpyruvate
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Synonyms

EC Number Synonyms Comment Organism
2.6.1.B17 HpgT
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Amycolatopsis orientalis
2.6.1.B17 L-4-hydroxyphenylglycine transaminase
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Amycolatopsis orientalis