Information on EC 2.3.2.B21 - cyclo(L-arginyl-L-tyrosyl) synthase

A0A397HK51

SwissProt

brenda

SwissProt

brenda

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GENERAL INFORMATION

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

physiological function

expression of AvaA in Escherichia coli or yeast with coexpression of yeast arginine-tRNA synthetase and tryptophan-tRNA synthetase leads to the synthesis of cyclo(L-arginyl-L-tyrosyl)

additional information

2 entries

additional information

A0A397HK51

enzyme has no sequence homology to non-ribosomal peptide synthetase or bacterial cyclodipeptide synthase

additional information

enzyme has no sequence homology to non-ribosomal peptide synthetase or bacterial cyclodipeptide synthase

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UNIPROT

ENTRY NAME

ORGANISM

NO. OF AA

NO. OF TRANSM. HELICES

MOLECULAR WEIGHT[Da]

SOURCE

SEQUENCE

LOCALIZATION PREDICTION

The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).

A0A397HK51 pBLAST

ANKA_ASPTH

518

58037

Swiss-Prot

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P9WEJ7 pBLAST

AVAA_ASPVE

541

60427

Swiss-Prot

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PROTEIN VARIANTS

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

C193A

mutation leads to complete loss of cyclodipeptide formation

C193S

mutation leads to complete loss of cyclodipeptide formation

C193T

mutation leads to complete loss of cyclodipeptide formation

D428A

mutation leads to complete loss of cyclodipeptide formation

D429A

mutation leads to complete loss of cyclodipeptide formation

E432A

mutation leads to complete loss of cyclodipeptide formation

Y392A

mutation leads to complete loss of cyclodipeptide formation

Y392F

mutation leads to complete loss of cyclodipeptide formation

Y515A

mutation leads to complete loss of cyclodipeptide formation

Y515F

about 11% of wild-type activity

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CLONED (Commentary)

ORGANISM

UNIPROT

LITERATURE

expressed in Aspergillus nidulans

2 entries

expressed in Aspergillus nidulans

A0A397HK51

expressed in Aspergillus nidulans

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