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Characterization of succinic semialdehyde dehydrogenase from Aspergillus niger

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Title Characterization of succinic semialdehyde dehydrogenase from Aspergillus niger
 
Creator KUMAR, S
KUMAR, S
PUNEKAR, NS
 
Subject SEMI-ALDEHYDE DEHYDROGENASE
SACCHAROMYCES-CEREVISIAE
RAT-BRAIN
4-AMINOBUTYRATE GABA
GAMMA-AMINOBUTYRATE
METABOLISM
PURIFICATION
SHUNT
Bi Bi mechanism
Enzyme kinetics
GABA metabolism
 
Description The catabolism of fungal 4-aminobutyrate (GABA) occurs via succinic semialdehyde (SSA). Succinic semialdehyde dehydrogenase (SSADH) from the acidogenic fungus Aspergillus niger was purified from GABA grown mycelia to the highest specific activity of 277 nmol min(-1) mg(-1), using phenyl Sepharose and DEAE Sephacel chromatography. The purified enzyme was specific for its substrates SSA and NAD(+). The substrate inhibition observed with SSA was uncompetitive with respect to NAD(+). While product inhibition by succinate was not observed, NADH inhibited the enzyme competitively with respect to NAD(+) and noncompetitively with respect to SSA. Dead-end inhibition by AMP and p-hydroxybenzaldehyde (pHB) was analyzed. The pHB inhibition was competitive with SSA and uncompetitive with NAD(+); AMP competed with NAD(+). Consistent with the kinetic data, a sequential, ordered Bi Bi mechanism is proposed for this enzyme.
 
Publisher NATL INST SCIENCE COMMUNICATION-NISCAIR
 
Date 2016-01-15T10:50:49Z
2016-01-15T10:50:49Z
2015
 
Type Article
 
Identifier INDIAN JOURNAL OF EXPERIMENTAL BIOLOGY, 53(2)67-74
0019-5189
0975-1009
http://dspace.library.iitb.ac.in/jspui/handle/100/18391
 
Language en