1975
DOI: 10.1093/oxfordjournals.jbchem.a130773
|View full text |Cite
|
Sign up to set email alerts
|

Studies on the Subsite Structure of Amylases

Abstract: Studies were made on the ultraviolet difference-spectra of glucoamylase from Rhizopus niveus [EC 3.2.1.3] specifically produced by the substrate maltose and the inhibitors, glucose, glucono-1: 5-lactone (gluconolactone), methyl beta-D-glucoside, cellubiose, and cyclohexa-, and cyclohepta-amyloses. Of these, maltose and gluconolactone produced characteristic difference spectra with a trough near 300 nm. Based on studies with a model compound for a tryptophan residue, Ac-Trp, this trough was attributed to the … Show more

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
2
1
1
1

Citation Types

1
11
0

Year Published

1977
1977
1990
1990

Publication Types

Select...
8
1

Relationship

2
7

Authors

Journals

citations
Cited by 35 publications
(12 citation statements)
references
References 0 publications
1
11
0
Order By: Relevance
“…•¬ (2) where KL' is the dissociation constant of glucono lactone from the ESL complex and 4Fmax is the maximum fluorescence intensity change that would be observed when the enzyme was saturated with * The subsites are numbered counting from the terminal one to which nonreducing end glucose residue of sub strates is bound in their productive binding modes.8)…”
Section: And Discussionmentioning
confidence: 99%
“…•¬ (2) where KL' is the dissociation constant of glucono lactone from the ESL complex and 4Fmax is the maximum fluorescence intensity change that would be observed when the enzyme was saturated with * The subsites are numbered counting from the terminal one to which nonreducing end glucose residue of sub strates is bound in their productive binding modes.8)…”
Section: And Discussionmentioning
confidence: 99%
“…Under the conditions employed, the total concen tration of the enzyme, [ 1.5 mm) (8), indicating that these three phenomena have the same origin. The binding of glucono lactone to the enzyme probably involves some change in the microenvironment of a tryptophan residue, which is considered to be situated at the first subsite (6,8). Kinetics of the Interaction- Figure 4 shows a typical example of the stopped-flow traces of the fluorescence change due to the interaction between the enzyme and the analog.…”
Section: And Discussionmentioning
confidence: 99%
“…Maltodextrin has been found to decrease the protein fluorescence intensity upon binding with the enzyme, and this property was used for a kinetic study of the interaction between the sub strate and the enzyme (9). Materials-Glucoamylase from Rhizopus niveus, maltose and gluconolactone were the same materials as those described in the previous paper (6). Gluconolactone solution was used within 15 min after dissolving to minimize its hydrolysis (8) and conversion to glucono-1, 4-lactone (10).…”
Section: Maltosementioning
confidence: 99%
“…G1ucoamy1ase is non-competitively inhibited by glucono1actone (65). This result, together with ultraviolet difference and fluorescence spectra indicate that glucono1actone is bound to the left of the catalytic site (66).…”
Section: Amylase Inhibitorsmentioning
confidence: 94%