Aspartic Acid 405 Contributes to the Substrate Specificity of Aminopeptidase B

Biochemistry ◽  
2006 ◽  
Vol 45 (38) ◽  
pp. 11425-11431 ◽  
Author(s):  
Kayoko M. Fukasawa ◽  
Junzo Hirose ◽  
Toshiyuki Hata ◽  
Yukio Ono
Keyword(s):  
Substrate Specificity ◽  
Aspartic Acid

scholarly journals A study of the metabolism of l-αγ-diaminobutyric acid in a Xanthomonas species

1969 ◽  
Vol 114 (1) ◽  
pp. 107-115 ◽  
Author(s):  
D. Rajagopal Rao ◽  
K. Hariharan ◽  
K. R. Vijayalakshmi
Keyword(s):  
Substrate Specificity ◽  
Aspartic Acid ◽  
Acid Metabolism ◽  
Ph Optimum ◽  
Diaminobutyric Acid ◽  
Oxaloacetic Acid ◽  
Binding Agents ◽  
Xanthomonas Species ◽  
High Degree

1. l-αγ-Diaminobutyric acid is metabolized in Xanthomonas sp. to aspartic β-semialdehyde, aspartic acid and oxaloacetic acid. 2. Aspartic β-semialdehyde is formed from diaminobutyric acid by a pyruvate-dependent γ-transamination. 3. The transaminase has a pH optimum of 9 and exhibits a high degree of substrate specificity, as analogues of diaminobutyric acid and pyruvate are inert in the system. The transaminase is inhibited by carbonyl-binding agents such as hydroxylamine. 4. Aspartic acid is formed from aspartic β-semialdehyde by an NAD+-dependent dehydrogenation. 5. The dehydrogenase has a pH optimum of 8·5 and is a thiol enzyme. It is specific for aspartic β-semialdehyde but analogues of NAD+ such as 3-acetylpyridine–adenine dinucleotide and deamino-NAD are partly active in the system. 6. The significance of these reactions is discussed in relation to diaminobutyric acid metabolism in plants and mammalian systems.

scholarly journals Identification of Aspartic Acid and Histidine Residues Mediating the Reaction Mechanism and the Substrate Specificity of the Human UDP-glucuronosyltransferases 1A

2007 ◽  
Vol 282 (50) ◽  
pp. 36514-36524 ◽  
Author(s):  
Dong Li ◽  
Sylvie Fournel-Gigleux ◽  
Lydia Barré ◽  
Guillermo Mulliert ◽  
Patrick Netter ◽  
...  
Keyword(s):  
Reaction Mechanism ◽  
Substrate Specificity ◽  
Aspartic Acid ◽  
Histidine Residues

Selective alteration of substrate specificity by replacement of aspartic acid-189 with lysine in the binding pocket of trypsin

Biochemistry ◽  
1987 ◽  
Vol 26 (9) ◽  
pp. 2616-2623 ◽  
Author(s):  
Laszlo Graf ◽  
Charles S. Craik ◽  
Andras Patthy ◽  
Steven Roczniak ◽  
Robert J. Fletterick ◽  
...  
Keyword(s):  
Substrate Specificity ◽  
Aspartic Acid ◽  
Binding Pocket

Substrate specificity and inducibility of TACE (tumour necrosis factor α-converting enzyme) revisited: the Ala-Val preference, and induced intrinsic activity

2003 ◽  
Vol 70 ◽  
pp. 39-52 ◽  
Author(s):  
Roy A. Black ◽  
John R. Doedens ◽  
Rajeev Mahimkar ◽  
Richard Johnson ◽  
Lin Guo ◽  
...  
Keyword(s):  
Substrate Specificity ◽  
Recent Work ◽  
Tumour Necrosis Factor ◽  
Tumour Necrosis ◽  
Transforming Growth Factor ◽  
Intrinsic Activity ◽  
Converting Enzyme ◽  
Tumour Necrosis Factor Α ◽  
Factor Α ◽  
Necrosis Factor

Tumour necrosis factor α (TNFα)-converting enzyme (TACE/ADAM-17, where ADAM stands for a disintegrin and metalloproteinase) releases from the cell surface the extracellular domains of TNF and several other proteins. Previous studies have found that, while purified TACE preferentially cleaves peptides representing the processing sites in TNF and transforming growth factor α, the cellular enzyme nonetheless also sheds proteins with divergent cleavage sites very efficiently. More recent work, identifying the cleavage site in the p75 TNF receptor, quantifying the susceptibility of additional peptides to cleavage by TACE and identifying additional protein substrates, underlines the complexity of TACE-substrate interactions. In addition to substrate specificity, the mechanism underlying the increased rate of shedding caused by agents that activate cells remains poorly understood. Recent work in this area, utilizing a peptide substrate as a probe for cellular TACE activity, indicates that the intrinsic activity of the enzyme is somehow increased.

Substrate Specificity of Leukocyte and Platelet Elastases

1978 ◽  
Vol 39 (03) ◽  
pp. 785-786 ◽  
Author(s):  
Y Legrand ◽  
J Caen ◽  
L Robert
Keyword(s):  
Substrate Specificity
Sign in / Sign up

Export Citation Format

Share Document