Evaluation of substrate promiscuity of an L-carbamoyl amino acid amidohydrolase from Geobacillus stearothermophilus CECT43

Biotechnology Progress

Volumn 26, Issue 4, 2010, Pages 954-959

  Pozo Dengra, Joaquín ^a   Martínez Gómez, Ana Isabel ^a   Martínez Rodríguez, Sergio ^a   Clemente Jiménez, Josefa María ^a   Rodríguez Vico, Felipe ^a   Heras Vázquez, Francisco Javier Las ^a  

^a UNIVERSITY OF ALMERÍA   (Spain)

Author keywords

Acylase process; Formylase process; Hydantoinase process; L amino acid production; L N carbamoylase; Substrate promiscuity

Indexed keywords

ACYLASE PROCESS; FORMYLASE PROCESS; HYDANTOINASE; L-AMINO ACIDS; N-CARBAMOYLASE;

AMINO ACIDS; BACTERIA; CHELATION; ENZYME ACTIVITY; ENZYME INHIBITION; ENZYMES; HYDROLYSIS; MANGANESE; MANGANESE COMPOUNDS; METAL IONS; ORGANIC ACIDS; POLYPEPTIDES; STEREOCHEMISTRY;

SUBSTRATES;

AMIDASE; N CARBAMOYLAMINO ACID AMIDOHYDROLASE; N-CARBAMOYLAMINO ACID AMIDOHYDROLASE;

ARTICLE; ENZYME SPECIFICITY; ENZYMOLOGY; GENETICS; GEOBACILLUS STEAROTHERMOPHILUS; METABOLISM; PH; TEMPERATURE;

AMIDOHYDROLASES; GEOBACILLUS STEAROTHERMOPHILUS; HYDROGEN-ION CONCENTRATION; SUBSTRATE SPECIFICITY; TEMPERATURE;

BACTERIA (MICROORGANISMS); GEOBACILLUS STEAROTHERMOPHILUS;

EID: 77956979591     PISSN: 87567938     EISSN: 15206033     Source Type: Journal    
DOI: 10.1002/btpr.410     Document Type: Article

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