ΠΠ»ΠΈΡΠ½ΠΈΠ΅ Π½Π΅ΠΎΡΠ³Π°Π½ΠΈΡΠ΅ΡΠΊΠΎΠ³ΠΎ ΡΠΎΡΡΠ°ΡΠ° ΠΈ ΠΊΠΎΡΠ΅ΡΠΌΠ΅Π½ΡΠ° Π½Π° ΡΠ΅ΡΠΌΠΎΡΡΠ°Π±ΠΈΠ»ΡΠ½ΠΎΡΡΡ Π½Π΅ΡΠΎΡΡΠΎΡΠΈΠ»ΠΈΡΡΡΡΠ΅ΠΉ Π³Π»ΠΈΡΠ΅ΡΠ°Π»ΡΠ΄Π΅Π³ΠΈΠ΄-3-ΡΠΎΡΡΠ°ΡΠ΄Π΅Π³ΠΈΠ΄ΡΠΎΠ³Π΅Π½Π°Π·Ρ
ΠΠΈΡΡΠ΅ΡΡΠ°ΡΠΈΡ
ΠΠ΅ΡΠΎΡΡΠΎΡΠΈΠ»ΠΈΡΡΡΡΠ°Ρ Π³Π»ΠΈΡΠ΅ΡΠ°Π»ΡΠ΄Π΅Π³ΠΈΠ΄-3-ΡΠΎΡΡΠ°ΡΠ΄Π΅Π³ΠΈΠ΄ΡΠΎΠ³Π΅Π½Π°Π·Π° (ΠΠ€ 1.2.1.9) (GAPN) ΠΊΠ°ΡΠ°Π»ΠΈΠ·ΠΈΡΡΠ΅Ρ Π½Π΅ΠΎΠ±ΡΠ°ΡΠΈΠΌΡΡ ΡΠ΅Π°ΠΊΡΠΈΡ ΠΎΠΊΠΈΡΠ»Π΅Π½ΠΈΡ Π³Π»ΠΈΡΠ΅ΡΠ°Π»ΡΠ΄Π΅Π³ΠΈΠ΄-3-ΡΠΎΡΡΠ°ΡΠ° Π² 3-ΡΠΎΡΡΠΎΠ³Π»ΠΈΡΠ΅ΡΠ°Ρ Ρ ΠΎΠ΄Π½ΠΎΠ²ΡΠ΅ΠΌΠ΅Π½Π½ΡΠΌ Π²ΠΎΡΡΡΠ°Π½ΠΎΠ²Π»Π΅Π½ΠΈΠ΅ΠΌ NAD (P): 3-Π€ΠΠ + NAD (P)+ + Π20 3-Π€Π + NAD (P)H + 2? t. ΠΡΠΎΡ ΡΠ΅ΡΠΌΠ΅Π½Ρ Π½Π°ΠΉΠ΄Π΅Π½ Π²ΠΎ Π²ΡΠ΅Ρ Π²ΡΡΡΠΈΡ ΡΠ°ΡΡΠ΅Π½ΠΈΡΡ , Π²ΠΎΠ΄ΠΎΡΠΎΡΠ»ΡΡ ΠΈ ΡΡΠ΄Π΅ ΠΌΠΈΠΊΡΠΎΠΎΡΠ³Π°Π½ΠΈΠ·ΠΌΠΎΠ². GAPN ΡΠ²Π»ΡΠ΅ΡΡΡ ΡΠ»Π΅Π½ΠΎΠΌ Π±ΠΎΠ»ΡΡΠΎΠ³ΠΎ ΡΡΠΏΠ΅ΡΡΠ΅ΠΌΠ΅ΠΉΡΡΠ²Π° Π°Π»ΡΠ΄Π΅Π³ΠΈΠ΄Π΅Π³ΠΈΠ΄ΡΠΎΠ³Π΅Π½Π°Π·… Π§ΠΈΡΠ°ΡΡ Π΅ΡΡ >
- Π‘ΠΎΠ΄Π΅ΡΠΆΠ°Π½ΠΈΠ΅
- ΠΡΠ΄Π΅ΡΠΆΠΊΠ°
- ΠΠΈΡΠ΅ΡΠ°ΡΡΡΠ°
- ΠΡΡΠ³ΠΈΠ΅ ΡΠ°Π±ΠΎΡΡ
- ΠΠΎΠΌΠΎΡΡ Π² Π½Π°ΠΏΠΈΡΠ°Π½ΠΈΠΈ
Π‘ΠΎΠ΄Π΅ΡΠΆΠ°Π½ΠΈΠ΅
- ΠΠΠΠΠ ΠΠΠ’ΠΠ ΠΠ’Π£Π Π«
- Π§Π°ΡΡΡ 1. ΠΠΎΠ½ΡΠ΅ΠΏΡΠΈΡ ΡΠ°Π·ΠΎΠ±ΡΠ΅Π½ΠΈΡ ΠΎΠΊΠΈΡΠ»Π΅Π½ΠΈΡ ΠΈ ΡΠΎΡΡΠΎΡΠΈΠ»ΠΈΡΠΎΠ²Π°Π½ΠΈΡ Π½Π° ΡΡΠ°Π΄ΠΈΠΈ Π³Π»ΠΈΠΊΠΎΠ»ΠΈΡΠΈΡΠ΅ΡΠΊΠΎΠΉ ΠΎΠΊΡΠΈΠ΄ΠΎΡΠ΅Π΄ΡΠΊΡΠΈΠΈ
- Π§Π°ΡΡΡ 2. ΠΠ±ΡΠ°Ρ Ρ Π°ΡΠ°ΠΊΡΠ΅ΡΠΈΡΡΠΈΠΊΠ° ΡΠΎΡΡΠ°ΡΠ°Π· 1,3-ΠΠΈΡΠΎΡΡΠΎΠ³Π»ΠΈΡΠ΅ΡΠ°ΡΠ°
- ΠΠΎΠ»ΠΈΡΡΠ±ΡΡΡΠ°ΡΠ½Π°Ρ Π°ΡΠΈΠ»ΡΠΎΡΡΠ°ΡΠ°Π·Π°
- Π€ΠΎΡΡΠΎΡΠΈΠ»ΠΈΡΡΡΡΠ°Ρ Π΄Π΅Π³ΠΈΠ΄ΡΠΎΠ³Π΅Π½Π°Π·Π° ΡΠΎΡΡΠΎΠ³Π»ΠΈΡΠ΅ΡΠΈΠ½ΠΎΠ²ΠΎΠ³ΠΎ Π°Π»ΡΠ΄Π΅Π³ΠΈΠ΄Π°, ΡΠΎΠ΄Π΅ΡΠΆΠ°ΡΠ°Ρ ΠΎΡΡΠ°ΡΠΎΠΊ ΡΡΠ»ΡΡΠ΅Π½ΠΎΠ²ΠΎΠΉ ΠΊΠΈΡΠ»ΠΎΡΡ Π² Π°ΠΊΡΠΈΠ²Π½ΠΎΠΌ ΡΠ΅Π½ΡΡΠ΅
- Π§Π°ΡΡΡ 3. Π‘ΡΡΡΠΊΡΡΡΠ½ΠΎ-ΡΡΠ½ΠΊΡΠΈΠΎΠ½Π°Π»ΡΠ½ΡΠ΅ ΠΎΡΠΎΠ±Π΅Π½Π½ΠΎΡΡΠΈ Π½Π΅ΡΠΎΡΡΠΎΡΠΈΠ»ΠΈΡΡΡΡΠΈΡ Π΄Π΅Π³ΠΈΠ΄ΡΠΎΠ³Π΅Π½Π°Π· 3-Π€ΠΠ
- Π€Π΅ΡΡΠ΅Π΄ΠΎΠΊΡΠΈΠ½-Π·Π°Π²ΠΈΡΠΈΠΌΡΠ΅ Π½Π΅ΡΠΎΡΡΠΎΡΡΠΈΡΡΡΡΠΈΠ΅ Π΄Π΅Π³ΠΈΠ΄ΡΠΎΠ³Π΅Π½Π°Π·Ρ ΡΠΎΡΡΠΎΠ³Π»ΠΈΡΠ΅ΡΠΈΠ½ΠΎΠ²ΠΎΠ³ΠΎ Π°Π»ΡΠ΄Π΅Π³ΠΈΠ΄Π°
- NAD (P)-3aeucuMbie Π½Π΅ΡΠΎΡΡΠΎΡΡΠΈΡΡΡΡΠΈΠ΅ Π΄Π΅Π³ΠΈΠ΄ΡΠΎΠ³Π΅Π½Π°Π·Ρ ΡΠΎΡΡΠΎΠ³Π»ΠΈΡΠ΅ΡΠΈΠ½ΠΎΠ²ΠΎΠ³ΠΎ Π°Π»ΡΠ΄Π΅Π³ΠΈΠ΄Π°: ΠΏΡΠΎΠΈΡΡ ΠΎΠΆΠ΄Π΅Π½ΠΈΠ΅, ΡΠ°ΡΠΏΡΠΎΡΡΡΠ°Π½Π΅Π½ΠΈΠ΅, ΡΡΡΡΠΊΡΡΡΠ° ΠΈ ΡΡΠ½ΠΊΡΠΈΡ
- Π Π΅Π°ΠΊΡΠΈΡ ΠΎΠΊΠΈΡΠ»Π΅Π½ΠΈΡ 3-Π€ΠΠ, ΠΊΠ°ΡΠ°Π»ΠΈΠ·ΠΈΡΡΠ΅ΠΌΠ°Ρ GAPN, ΡΡΠ±ΡΡΡΠ°ΡΡ ΠΈ ΠΈΠ½Π³ΠΈΠ±ΠΈΡΠΎΡΡ ΡΠ΅ΡΠΌΠ΅Π½ΡΠ°
- Π‘ΡΡΡΠΊΡΡΡΠ° NAD (P)-3aBHCHMofi Π½Π΅ΡΠΎΡΡΠΎΡΠΈΠ»ΠΈΡΡΡΡΠ΅ΠΉ Π³Π»ΠΈΡΠ΅ΡΠ°Π»ΡΠ΄Π΅Π³ΠΈΠ΄-3-ΡΠΎΡΡΠ°Ρ Π΄Π΅Π³ΠΈΠ΄ΡΠΎΠ³Π΅Π½Π°Π·Ρ
- Π Π°ΡΠΏΡΠΎΡΡΡΠ°Π½Π΅Π½ΠΈΠ΅ ΠΈ ΠΏΡΠΎΠΈΡΡ ΠΎΠΆΠ΄Π΅Π½ΠΈΠ΅ Π½Π΅ΡΠΎΡΡΠΎΡΠΈΠ»ΠΈΡΡΡΡΠ΅ΠΉ Π€ΠΠΠ΄Π΅Π³ΠΈΠ΄ΡΠΎΠ³Π΅Π½Π°Π·Ρ
- Π€ΠΈΠ·ΠΈΠΎΠ»ΠΎΠ³ΠΈΡΠ΅ΡΠΊΠ°Ρ ΡΠΎΠ»Ρ GAPN Ρ ΡΠ°Π·Π»ΠΈΡΠ½ΡΡ ΠΎΡΠ³Π°Π½ΠΈΠ·ΠΌΠΎΠ²
- ΠΡΠΎΠ±Π΅Π½Π½ΠΎΡΡΠΈ ΡΡΡΠΎΠ΅Π½ΠΈΡ Π°ΠΊΡΠΈΠ²Π½ΠΎΠ³ΠΎ ΡΠ΅Π½ΡΡΠ° ΠΈ ΠΌΠ΅Ρ Π°Π½ΠΈΠ·ΠΌ ΠΊΠ°ΡΠ°Π»ΠΈΠ·Π° NADP-Π·Π°Π²ΠΈΡΠΈΠΌΠΎΠΉ Π½Π΅ΡΠΎΡΡΠΎΡΠΈΠ»ΠΈΡΡΡΡΠ΅ΠΉ Π΄Π΅Π³ΠΈΠ΄ΡΠΎΠ³Π΅Π½Π°Π·Ρ 3ΡΠΎΡΡΠΎΠ³Π»ΠΈΡΠ΅ΡΠΈΠ½ΠΎΠ²ΠΎΠ³ΠΎ Π°Π»ΡΠ΄Π΅Π³ΠΈΠ΄Π° ΠΈΠ· Streptococcus mutans
- Π‘ΡΡΡΠΊΡΡΡΠ° Π°ΠΏΠΎ- ΠΈ Ρ ΠΎΠ»ΠΎ-ΡΠ΅ΡΠΌΠ΅Π½ΡΠ° ΠΏΠΎ Π΄Π°Π½Π½ΡΠΌ ΠΊΡΠΈΡΡΠ°Π»Π»ΠΎΠ³ΡΠ°ΡΠΈΡΠ΅ΡΠΊΠΈΡ ΠΈΡΡΠ»Π΅Π΄ΠΎΠ²Π°Π½ΠΈΠΉ
- ΠΠ»ΠΈΡΠ½ΠΈΠ΅ ΡΠ°Π·Π»ΠΈΡΠ½ΡΡ ΠΌΡΡΠ°ΡΠΈΠΉ Π² ΠΎΠ±Π»Π°ΡΡΠΈ Π°ΠΊΡΠΈΠ²Π½ΠΎΠ³ΠΎ ΡΠ΅Π½ΡΡΠ° Π½Π° ΠΊΠ°ΡΠ°Π»ΠΈΡΠΈΡΠ΅ΡΠΊΠΈΠ΅ ΡΠ²ΠΎΠΉΡΡΠ²Π° GAPN S. mutans
- ΠΠΈΠΏΠΎΡΠ΅ΡΠΈΡΠ΅ΡΠΊΠ°Ρ ΡΡ Π΅ΠΌΠ° ΠΊΠ°ΡΠ°Π»ΠΈΠ·Π°, ΠΎΡΡΡΠ΅ΡΡΠ²Π»ΡΠ΅ΠΌΠΎΠ³ΠΎ GAPN S. mutans
- ΠΠΠ‘ΠΠΠ ΠΠΠΠΠ’ΠΠΠ¬ΠΠΠ― Π§ΠΠ‘Π’
- ΠΠΠ’ΠΠ ΠΠΠΠ« Π ΠΠΠ’ΠΠΠ«
- ΠΡΠ΄Π΅Π»Π΅Π½ΠΈΠ΅ GAPN Streptococcus mutans
- ΠΠΎΠ»ΡΡΠ΅Π½ΠΈΠ΅ ΡΠΈΡΠΎΠΏΠ»Π°Π·ΠΌΠ°ΡΠΈΡΠ΅ΡΠΊΠΎΠΉ ΡΡΠ°ΠΊΡΠΈΠΈ ΡΠ΅ΡΠΌΠ΅Π½ΡΠΎΠ² ΠΈΠ· ΠΌΡΡΡ ΠΊΡΡΡΡ
- ΠΠ½Π°Π»ΠΈΡΠΈΡΠ΅ΡΠΊΠΈΠ΅ ΠΌΠ΅ΡΠΎΠ΄Ρ
- ΠΠΏΡΠ΅Π΄Π΅Π»Π΅Π½ΠΈΠ΅ ΡΠΎΡΠ½ΡΡ ΠΊΠΎΠ½ΡΠ΅Π½ΡΡΠ°ΡΠΈΠΉ Π½Π΅ΠΊΠΎΡΠΎΡΡΡ ΡΠ΅Π°Π³Π΅Π½ΡΠΎΠ²
- ΠΠΏΡΠ΅Π΄Π΅Π»Π΅Π½ΠΈΠ΅ ΠΊΠΎΠ½ΡΠ΅Π½ΡΡΠ°ΡΠΈΠΉ Π±Π΅Π»ΠΊΠΎΠ²
- ΠΠΏΡΠ΅Π΄Π΅Π»Π΅Π½ΠΈΠ΅ ΠΊΠΎΠ½ΡΠ΅Π½ΡΡΠ°ΡΠΈΠΈ Π»Π°ΠΊΡΠ°ΡΠ° Π² ΠΌΡΡΠ΅ΡΠ½ΠΎΠΌ ΡΠΊΡΡΡΠ°ΠΊΡΠ΅
- ΠΠΏΡΠ΅Π΄Π΅Π»Π΅Π½ΠΈΠ΅ ΡΠ΅ΡΠΌΠ΅Π½ΡΠ°ΡΠΈΠ²Π½ΠΎΠΉ Π°ΠΊΡΠΈΠ²Π½ΠΎΡΡΠΈ ΠΠΠ€Π ΠΈ GAPN
- ΠΠΏΡΠ΅Π΄Π΅Π»Π΅Π½ΠΈΠ΅ ΡΠΎΡΡΠ°ΡΠ° Π² ΠΏΡΠ΅ΠΏΠ°ΡΠ°ΡΠ°Ρ GAPN
- ΠΠΎΠ΄ΠΈΡΠΈΠΊΠ°ΡΠΈΡ ΡΡΠ»ΡΡΠ³ΠΈΠ΄ΡΠΈΠ»ΡΠ½ΡΡ Π³ΡΡΠΏΠΏ ΠΠΠ€Π ΠΈ GAPN, ΠΏΡΠΈ ΠΏΠΎΠΌΠΎΡΠΈ
- ΠΠ’ΠΠ
- ΠΠ½Π°ΠΊΡΠΈΠ²Π°ΡΠΈΡ ΠΠΠ€Π ΠΈ GAPN ΡΠ΅Π°Π³Π΅Π½ΡΠ°ΠΌΠΈ Π½Π° ΡΡΠ»ΡΡΠ³ΠΈΠ΄ΡΠΈΠ»ΡΠ½ΡΠ΅ Π³ΡΡΠΏΠΏΡ
- ΠΠ»Π΅ΠΊΡΡΠΎΡΠΎΡΠ΅Π· Π±Π΅Π»ΠΊΠΎΠ² Π² ΠΏΠΎΠ»ΠΈΠ°ΠΊΡΠΈΠ»Π°ΠΌΠΈΠ΄Π½ΠΎΠΌ Π³Π΅Π»Π΅
- ΠΠΈΡΡΠ΅ΡΠ΅Π½ΡΠΈΠ°Π»ΡΠ½Π°Ρ ΡΠΊΠ°Π½ΠΈΡΡΡΡΠ°Ρ ΠΊΠ°Π»ΠΎΡΠΈΠΌΠ΅ΡΡΠΈΡ
- Π Π΅Π³ΠΈΡΡΡΠ°ΡΠΈΡ ΡΠΏΠ΅ΠΊΡΡΠΎΠ² ΠΊΡΡΠ³ΠΎΠ²ΠΎΠ³ΠΎ Π΄ΠΈΡ ΡΠΎΠΈΠ·ΠΌΠ°
- Π ΠΠΠ£ΠΠ¬Π’ΠΠ’Π« Π ΠΠΠ‘Π£ΠΠΠΠΠΠ
- Π§Π°ΡΡΡ 1. ΠΠ½Π΄ΡΡΠΈΡΠΎΠ²Π°Π½Π½ΡΠΉ Π°Π½ΠΈΠΎΠ½Π°ΠΌΠΈ ΠΏΠ΅ΡΠ΅Ρ ΠΎΠ΄ ΠΌΠ΅ΠΆΠ΄Ρ Π΄Π²ΡΠΌΡ ΡΠΎΡΠΌΠ°ΠΌΠΈ Π½Π΅ΡΠΎΡΡΠΎΡΠΈΠ»ΠΈΡΡΡΡΠ΅ΠΉ Π³Π»ΠΈΡΠ΅ΡΠ°Π»ΡΠ΄Π΅Π³ΠΈΠ΄-3-ΡΠΎΡΡΠ°Ρ Π΄Π΅Π³ΠΈΠ΄ΡΠΎΠ³Π΅Π½Π°Π·Ρ
- ΠΠ±Π½Π°ΡΡΠΆΠ΅Π½ΠΈΠ΅ Π΄Π²ΡΡ ΡΠΎΡΠΌ Π°ΠΏΠΎΡΠ΅ΡΠΌΠ΅Π½ΡΠ° Π΄ΠΈΠΊΠΎΠ³ΠΎ ΡΠΈΠΏΠ°, ΡΠ°Π·Π»ΠΈΡΠ°ΡΡΠΈΡ ΡΡ ΠΏΠΎ ΡΠ΅ΡΠΌΠΎΡΡΠ°Π±ΠΈΠ»ΡΠ½ΠΎΡΡΠΈ ΠΈ ΡΠ»Π΅ΠΊΡΡΠΎΡΠΎΡΠ΅ΡΠΈΡΠ΅ΡΠΊΠΎΠΉ ΠΏΠΎΠ΄Π²ΠΈΠΆΠ½ΠΎΡΡΠΈ. 74 ΠΠ»ΠΈΡΠ½ΠΈΠ΅ ΡΠ ΡΡΠ΅Π΄Ρ Π½Π° Ρ Π°ΡΠ°ΠΊΡΠ΅Ρ ΡΠ΅ΡΠΌΠΎΠ³ΡΠ°ΠΌΠΌ Π°ΠΏΠΎΡΠ΅ΡΠΌΠ΅Π½ΡΠ° GAPN Π΄ΠΈΠΊΠΎΠ³ΠΎ ΡΠΈΠΏΠ°
- ΠΠΎΠ·ΠΌΠΎΠΆΠ½ΡΠΉ ΡΡΠ°ΡΡΠΎΠΊ ΡΠ²ΡΠ·ΡΠ²Π°Π½ΠΈΡ Π°Π½ΠΈΠΎΠ½Π° Ρ ΠΌΠΎΠ»Π΅ΠΊΡΠ»ΠΎΠΉ GAPN
- Π‘Π²ΠΎΠΉΡΡΠ²Π° ano-GAPN Π² Π³Π»ΠΈΡΠΈΠ½ΠΎΠ²ΠΎΠΌ Π±ΡΡΠ΅ΡΠ΅
- ΠΠ΅Π·Π°Π²ΠΈΡΠΈΠΌΠ°Ρ ΡΠ΅ΡΠΌΠΎΠ΄Π΅Π½Π°ΡΡΡΠ°ΡΠΈΡ ΡΠΎΡΠΌΡ Π
- ΠΠ»ΠΈΡΠ½ΠΈΠ΅ ΡΠΎΡΡΠ°ΡΠ° Π½Π° Π΄ΠΎΡΡΡΠΏΠ½ΠΎΡΡΡ ΠΎΡΡΠ°ΡΠΊΠΎΠ² ΡΠΈΡΡΠ΅ΠΈΠ½Π° GAPN ΠΊ Ρ ΠΈΠΌΠΈΡΠ΅ΡΠΊΠΎΠΉ ΠΌΠΎΠ΄ΠΈΡΠΈΠΊΠ°ΡΠΈΠΈ
Π‘ΠΏΠΈΡΠΎΠΊ Π»ΠΈΡΠ΅ΡΠ°ΡΡΡΡ
- ΠΡΡΠΎΠ½Π΅Ρ Π.Π., Π€ΠΎΠΊΠΈΠ½Π° Π. Π., Π¨ΠΌΠ°Π»ΡΠ³Π°ΡΠ·Π΅Π½ Π. Π. (1999) Π ΠΎΠ»Ρ Π³Π»ΠΈΡΠ΅ΡΠ°Π»ΡΠ΄Π΅Π³ΠΈΠ΄-3-ΡΠΎΡΡΠ°Ρ Π΄Π΅Π³ΠΈΠ΄ΡΠΎΠ³Π΅Π½Π°Π·Ρ Π² ΡΠ΅Π³ΡΠ»ΡΡΠΈΠΈ Π³Π»ΠΈΠΊΠΎΠ»ΠΈΠ·Π°. Π£ΡΠΏΠ΅Ρ ΠΈ Π±ΠΈΠΎΠ». Ρ ΠΈΠΌΠΈΠΈ XXXIX: 77−103
- ΠΠ°Π³ΡΠ°Π΄ΠΎΠ²Π° Π.Π. (2001) ΠΠ·ΡΡΠ΅Π½ΠΈΠ΅ ΡΠ²ΠΎΠΉΡΡΠ² ΡΠΎΡΡΠΎΡΠΈΠ»ΠΈΡΡΡΡΠ΅ΠΉ D-Π³Π»ΠΈΡΠ΅ΡΠ°Π»ΡΠ΄Π΅Π³ΠΈΠ΄-3-ΡΠΎΡΡΠ°Ρ Π΄Π΅Π³ΠΈΠ΄ΡΠΎΠ³Π΅Π½Π°Π·Ρ. ΠΠΈΠΎΡ ΠΈΠΌΠΈΡ 66(10): 13 231 335
- Π¦ΠΎΡ Π§.-Π. (1998) Π ΠΎΠ»Ρ Π³ΠΈΠ±ΠΊΠΎΡΡΠΈ Π°ΠΊΡΠΈΠ²Π½ΠΎΠ³ΠΎ ΡΠ΅Π½ΡΡΠ° Π² ΡΠ΅ΡΠΌΠ΅Π½ΡΠ°ΡΠΈΠ²Π½ΠΎΠΌ ΠΊΠ°ΡΠ°Π»ΠΈΠ·Π΅. ΠΠΈΠΎΡ ΠΈΠΌΠΈΡ 63(3): 300−307
- Allison W.S., and Connors M.J. (1970) The activation and inactivation of the acyl phosphatase activity of glyceraldehyde-3-phosphate dehydrogenase. Arch. Biochem. Biophys. 136: 383−391
- Arnon D.I., Rosenberg L.L., Whatley F.R. (1954) A new glycerol dehyde-3-phospate dehydrogenase from photosynthetic tissues. Nature 173: 11 321 134
- Bamberger E.S., Ehrlich B.A. and Gibbs M. (1975) The glyceraldehyde-3-phosphate and glycerate-3-phosphate shuttle and carbon dioxide assimilation in intact spinach chloroplasts. Plant Physiol 55: 1023−1030
- Boyd D.A., Cvitkovitch D.G., Hamilton I.R. (1995) Sequence, expression and function of the gene for the non-phosphorylating, NADP-dependent glyceraldehyde-3-phospate dehydrogenase of Streptococcus mutans. J. Bacteriol. 177 (10): 2622−2627
- Brown A.T., Wittenberger C.L. (1971) The occurrence of multiple glyceraldehydes-3-phosphate dehydrogenases in cariogenic streptococci. Biochem. Biophys. Research Communications 43(1): 217−224
- Casati D.F.G., Sesma J.I., Iglesias A.A. (2000) Structural and kinetic characterization of NADP-dependent non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase from celery leaves. Plant Science 154: 107−115
- Chiarugi P., Degl’Innocenti D., Raugei G., Fiaschi Π’., Ramponi G. (1997) Differential migration of acylphosphatase isoenzymes from cytoplasm to nucleus during apoptotic cell death. Biochem. Biophys. Res. Commun. 231(3): 717−21
- Chiarugi P., Raugei G., Marzocchini R., Fiaschi Π’., Ciccarelli C., Berti A. et al. (1995) Differential modulation of expression of the two acylphosphatase isoenzymes by thyroid hormone. Biochem. J. 311: 567 573
- Chiti F., Taddei N., Stefani M., Dobson C.M., Ramponi G. (2001) Reduction of the amyloidogenicity of a protein by specific binding of ligands to the native conformation. Protein Sci. 10(4): 879−86
- Chiti F., Webster P., Taddei N., Clark A., Stefani M., Ramponi G., Dobson C.M. (1999) Designing conditions for in vitro formation of amyloid protofilaments and fibrils. Proc. Nat. Acad. Sci. USA 96(7): 3590−4
- Cobessi, D., Tete Favier, F., Marchal, S., Azza, S., Branlant, G., Aubry, A. (1999) Apo and holo crystal structures of a NADP-dependent aldehyde dehydrogenase from Streptococcus mutans. J. Mol. Biol. 290: 161−173
- Cobessi, D., Tete Favier, F., Marchal, S., Branlant, G., Aubry, A. (2000) Structural and biochemical investigations of the catalytic mechanism of an NADP-dependent aldehyde dehydrogenase from Streptococcus mutans. J. Mol. Biol. 300: 141−152
- Cogan E.B., Birrell G.B., Griffith O.H. (1999) A robotics-based automatic assays for inorganic and organic phosphates. Anal. Biochem. 271(1): 29−35
- Crow V.L., Wittenberger Π‘. L. (1979) Separation and properties of NAD-and NADP-dependent glyceraldehydes-3-phosphate dehydrogenases from Streptococcus mutans. J. Biol. Chem. 254: 1134−1142
- D’Amico S., Gerday C., and Feller G. (2001) Structural determinants of cold adaptation and stability in a large protein. J. Biol. Chem. 276(28): 25 791−25 796
- Damaschun G., Damaschun H., Gast K., Zirwer D. (1999) Proteins can adopt totally different folded conformations. J. Mol. Biol. 291: 715−725
- Farres J., Wang T.T., Cunningham S.J., Weiner H. (1995) Investigation of the active site cysteine residue of rat liver mitochondrial aldehyde dehydrogenase by site-directed mutagenesis. Biochemistry 34(8): 2592−8
- Farres J., Wang T.T.Y., Cunningam S.J., Weiner H. (1995) Investigation of the active site cysteine residue of rat liver mitochondrial aldehyde dehydrogenase by site directed mutagenesis. Biochemistry 34: 2592−2598
- Fedor L.R., Bruice T.C. (1964) Nucleophilic displacement reactions at the thiolester bond. II. Hydrazinolysis and morpholinolysis in aqueous solutions. J. Am. Chem. Soc. 86: 4117−4123
- Feher V.A., Cavanagh J. (1999) Millisecond-timescale motions contribute to the function of the bacterial response regulator protein SpoOF. Nature 400(6741): 289−93
- Forman-Kay J.D. (1999) The «dynamics» in the thermodynamics of binding. Nature Struct. Biol. 6(12): 1086−7
- Gerday C., Aittaleb M., Arpigny J.L., Baise E., Chessa J-P., Garsoux G., Petrescu I., Feller G. (1997) Psychrophilic enzymes: a thermodynamic challenge. Biochim. Biophys. Acta 1342: 119−131
- Giannoni E., Cirri P., Paoli P., Fischi Π’., Camici G., Manao G., Raugei G., Ramponi G. (2000) Acylphosphatase is a strong apoptosis inducer in HeLa cell line. Moll. Cell. Biol. Res. Commun. 3(5): 264−70
- Habenicht A., Hellman U., Cerff R. (1994) Non-phosphorylating GAPDH of higher plants is a member of the aldehyde dehydrogenase superfamily with no sequence homology to phosphorylating GAPDH. J. Mol. Biol. 237(1): 165−71
- Habenicht A. (1997) The non-phosphorylating glyceraldehyde-3-phospate dehydrogenase: biochemistry, structure, occurence and evolution. Biological chemistry 378: 1413−1419
- Habenicht A., Quesada A., Cerff R. (1997) Sequence of the non-phosphorylating glyceraldehyde-3-phospate dehydrogenase from Nicotiana plumbaginifolia and phylogenetic origin of the family. Gene 198(1−2): 237−243
- Hammen P.K., Allali-Hassani A., Hallenga K., Hurley T.D., Weiner H. (2002) Multiple conformations of NAD and NADH when bound to human cytosolic and mitochondrial aldehyde dehydrogenase. Biochemistry 41(22): 7156−68
- Harary I. (1957) The hydrolysis of 1,3-diphosphoglyceric acid by acylphosphatase. Biochim. Biophys. Acta 26: 434−436
- Hempel J., Perozich J., Chapman Π’., Rose J., Boesch J.S., Liu Z.J., Lindahl R., Wang B.C. (1999) Aldehyde dehydrogenase catalytic mechanism. A proposal. Adv. Exp. Med. Biol. 463: 53−9
- Hensel R., Laumann S., Lang J., Heumann H., and Lottspeich F. (1987) Characterization of two D-glyceraldehyde-3-phosphate dehydrogenases from the extremely thermophilic archaebacterium Thermoproteus tenax. Eur. J. Biochem. 170: 325−333
- Hokin L.E., Sastry P. S., Galsworthy P.R. and Yoda A. (1965) Evidence that a phosphorylated intermediate in a brain transport adenosine triphosphatase is an acylphosphate. Proc. Natl. Acad. Sci. USA 54: 177— 184
- Hu Y., Faham S., Roy R., Adams M.W.W. and Rees D.C. (1999) Formaldehyde ferredoxin oxidoreductase from Pyrococcus furiosus: the 1.85 A resolution crystal structure and its mechanistic implications. J. Mol. Biol. 286: 899−914
- Hurley T.D., Steinmetz C.G., Weiner H. (1999) Three-dimensional structure of mitochondrial aldehyde dehydrogenase. Mechanistic implications. Adv. Exp. Med. Biol. 463: 15−25
- Hurley T.D., Weiner H. (1999) Evaluation of the roles of the conserved residues of aldehyde dehydrogenase. Adv. Exp. Med. Biol. 463: 45−52
- Iglesias A. A, Losada M. (1988) Purification and kinetic and structural properties of spinach leaf NADP-dependent nonphosphorylating glyceraldehyde-3-phosphate dehydrogenase. Arch. Biochem. Biophys. 260(2): 830−40
- Iglesias A.A., Serrano A., Guerrero M.G. and Losada M. (1987) Purification and properties of NADP-dependent non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase from the green alga Chlamydomonas reinhardtii. Biochim. Biophys. Acta 925: 1−10
- Johansson K., El-Ahmad M., Ramaswamy S., Hjelmqvist L., Jornvall H., Eklund H. (1998) Structure of betaine aldehyde dehydrogenase at 2.1A resolution. Protein Sci. 7: 2106−2117
- Kelly G.J. and Gibbs M. (1973a) Nonreversible D-glyceraldehyde-3-phosphate dehydrogenase of plant tissue. Plant Physiol. 52: 111−118
- Kelly G.J. and Gibbs M. (1973b) A mechanism of the indirect transfer of photosynthetically reduced nicotinamide adenine dinucleotide phosphate from the chloroplast to the cytoplasm. Plant Physiol. 52: 674−676
- Kengen S.W.M., de Vos W.M., Stams A.J.M. (1996) Sugar metabolism ofhyperthermophiles. FEMS Microbiology reviews 18: 119−137
- Kengen S.W., Tuininga J.E., de Bok F.A., Stams A.J., de Vos W.M. (1995) Purification and characterization of a novel ADP-dependent glucokinase from the hyperthermophilic archaeon Pyrococcus furiosus. J. Biol. Chem. 270(51): 30 453−7
- Khoroshilova N.A., Muronetz V.I., Nagradova N.K. (1992) Interaction between D-glyceraldehyde-3-phosphate dehydrogenase and 3phosphoglycerate kinase and its functional consequences. FEBS Lett. 297(3): 247−9
- Kitson T.M. and Kitson K.E. (1996) A comparison of nitrophenyl esters and lactones as substrates of cytosolic aldehyde dehydrogenase. Biochem. J. 316: 225−232
- Kitson T.M. and Kitson K.E. (1997) Studies of the esterase activity of cytosolic aldehyde dehydrogenase with resorufm acetate as substrate Biochem. J. 322: 701−708
- Kuzminskaya E.V., Asryants R.A., Nagradova N.K. (1991) Rabbit muscle tetrameric D-glyceraldehyde-3-phosphate dehydrogenase is locked in the asymmetric state by chemical modification of a single arginine per subunit. Biochim. Biophys. Acta 1075: 123−130
- Laemmli U.K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227: 680−685
- Lamb A.L., Newcomer M.E. (1999) The structure of retinal dehydrogenase type II at 2.7 A resolution: implications for retinal specificity. Biochemistry 38(19): 6003−11
- Liguri G., Cecchi C., Latorraca S., Pieri A., Sorbi S., Degl’In-nocenti D. et al. (1996) Alteration of acylphosphatase levels in familial Alzheimer’sdisease fibroblasts with presenilin gene mutations. Neurosci. Lett. 210: 153−156
- Lindahl R. (1992) Aldehyde dehydrogenases and their role in carcinogenesis. Crit. Rev. Biochem. Mol. Biol. 27(4−5): 283−335
- Lipmann F. (1946) Acetylphosphate. Adv. Enzymol. 6: 231−267
- Loh A.P., Guo W., Nicholson L.K., Oswald R.E. (1999) Backbone dynamics of inactive, active, and effector-bound Cdc42Hs from measurements of (15)N relaxation parameters at multiple field strengths. Biochemistry 38(39): 12 547−57
- Loh A.P., Pawley N., Nicholson L.K., Oswald R.E. (2001) An increase in side chain entropy facilitates effector binding: NMR characterization of the side chain methyl group dynamics in Cdc42Hs. Biochemistry 40(15): 4590−600.
- Lonhienne Π’., Gerday C., Feller G. (2000) Psychrophilic enzymes: revisiting the thermodynamic parameters of activation may explain local flexibility. Biochim. Biophys. Acta 1543: 1−10
- Mann C.J., Weiner H. (1999) Differences in the roles of conserved glutamic acid residues in the active site of human class 3 and class 2 aldehyde dehydrogenases. Protein Sci. 8(10): 1922−9
- Mann K. and Mecke D. (1979) Inhibition of spinach glyceraldehyde-3-phosphate dehydrogenases by pentalenolactone. Nature 282: 535−536
- Mann C.J., Weiner H. (1999) Differences in the roles of conserved glutamic acid residues in the active site of human class 3 and class 2 aldehyde dehydrogenase. Protein Sci. 8: 1922−1929
- Marchal S., Cobessi D., Rahuel-Clermont S., Tete-Favier F., Aubry A., Branlant G. (2001) Chemical mechanism and substrate binding sites of NADP-dependent aldehyde dehydrogenase from Streptococcus mutans. Chemico-Biological Interactions 130−132: 15−28
- Marchal S. and Branlant G. (2001) Engineered nonphosphorylating glyceraldehyde-3-phosphate dehydrogenase at position 268 binds hydroxylamine and hydrazine as acyl acceptors. Eur. J. Biochem. 268: 5764−5770
- Marchal S. and Branlant G. (2002) Characterization of the amino acids involved in substrate specificity of non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase from Streptococcus mutans. J. Biol. Chem. 277(42): 39 235−42
- Marchal S., Branlant G. (1999) Evidence for the chemical activation of essential Cys-302 upon cofactor binding to nonphosphorylating glyceraldehyde 3-phosphate dehydrogenase from Streptococcus mutans. Biochemistry 38: 12 950−12 958
- Marchal S., Rahuel-Clermont S., Branlant G., (2000) The role of Glu268 in the catalytic mechanism of non-phosphorylating glyceraldehyde dehydrogenase from Streptococcus mutans. Biochemistry 39: 3327−3335
- Mateos M.I. and Serrano A. (1992) Occurense of phosphorylating and non-phosphorylating NADP-dependent glyceraldehyde-3-phosphate dehydrogenases in photosynthetic organisms. Plant Science 84: 163−170
- Mateos M.I., Serrano A. (1992) Occurence of phosphorylating and nonphosphorylating NADP-dependent glyceraldehyde-3-phospate dehydrogenases in photosynthetic organisms. Plant Science 84: 163−170
- Meyerhof O. (1994 1948.) New investigations on enzymatic glycolysis and phosphorylation. Experientia 50: 382−389
- Michels S., Scagliarini S., Delia Seta F., Carles C., Riva M., Trost P., Branlant G. (1994) Arguments against a close relationship between nonphosphorylating and phosphorylating glyceraldehyde-3-phosphate dehydrogenases. FEBS Lett. 339(1−2): 97−100
- Moore S.A., Baker H.M., Blythe T.J., Kitson K.E., Kitson T.M., Baker E.N. (1998) Sheep liver cytosolic aldehyde dehydrogenase: the structure reveals the basis for the retinal specificity of class 1 aldehyde dehydrogenases. Structure 6(12): 1541−51
- Moore S.A., Baker H.M., Blythe T.J., Kitson K.E., Kitson T.M., Baker E.N. (1998) Sheep liver cytosolic aldehyde dehydrogenase: the structure reveals the basis for the retinal specificity of class 1 aldehyde dehydrogenases. Structure 6: 1541−1551
- Mukund S., and Adams M.W.W. (1995) Glyceraldehyde-3-phosphate ferredoxin oxidoreductase, a novel tungsten-containing enzyme with a potential glycolytic role in the hyperthermophilic archaeon, Pyrococcus furiosus. J. Biol. Chem. 270: 8389−8392
- Muronetz V.I., Wang Z.X., Keith T.J., Knull H.R., Srivastava D.K. (1994) Binding constants and stoichiometrics of glyceraldehyde 3-phosphate dehydrogenase-tubulin complexes. Arch. Biochem. Biophys. 313(2): 253−60
- Nakano M.M., Zhu Y., Haga K., Yoshikawa H., Sonenshein A.L. and Zuber P. (1999) A mutation in the 3-phosphoglycerate kinase gene allows anaerobic growth of Bacillus subtilis in the absence of ResE kinase. J. Bacterid. 181(22): 7087−7097
- Nassi P., Liguri G., Landi N., Berti A., Stefani M., Pavolini B. et al. (1985) Acylphosphatase from human skeletal muscle: purification, some properties and levels in normal and my-opathic muscles. Biochem. Med. 34:166−175
- Nassi P., Liguri G., Nediani C., Taddei N., Piccinni P., Degl’Innocenti D. et al. (1989) Increased acylphosphatase levels in erythrocytes from hyperthyroid patients. Clin. Chim. Acta 183: 351−358
- Nassi P., Marchetti E., Nediani C., Liguri G. and Ramponi G. (1993) Acylphosphatase induced modifications in the fimc-tional properties of erythrocyte membrane sodium pump. Biochim. Biophys. Acta 1147: 1926
- Nassi P., Nediani C., Fiorillo C., Marchetti E., Liguri G. And Ramponi G. (1994) Modifications induced by acylphosphatase in the functional properties of heart sarcolemma Na Π + pump. FEBS Lett. 337: 109−113
- Nassi P., Nediani C., Liguri G., Taddei N. and Ramponi G. (1991) Effects of acylphosphatase on the activity of erythro-cyte membrane Ca2+ pump. J. Biol. Chem. 266: 10 867−10 871
- Nediani C., Fiorillo C., Marchetti E., Pacini A., Liguri G. and Nassi P. (1996) Stimulation of cardiac sarcoplasmic reticulum calcium pump by acylphosphatase. J. Biol. Chem. 271: 19 066−19 073
- Ni L., Sheikh S., Weiner H. (1997) Involvement of glutamate 399 and lysine 192 in the mechanism of human liver mitochondrial aldehyde dehydrogenase. J. Biol. Chem. 272(30): 18 823−6
- Ouellet M., Shoubridge E.A. (1992) Phosphocreatine-dependent protein phosphorylation in rat skeletal muscle. Biochem. J. 284 (Pt 1): 115−22
- Paoli P., Camici G., Manao G., Giannoni E., Ramponi G. (2000) Acylphosphatase possesses nucleoside triphosphatase and nucleoside diphosphatase activities. Biochem. J. 349 (Ptl): 43−9
- Parker D.J., and Allison W.S. (1969) The mechanism of inactivation of glyceraldehyde 3-phosphate dehydrogenase by tetrathionate, o-iodozobenzoate, and iodine monochloride. J. Biol. Chem. 244: 180−189
- Pastore A., Saudek V., Ramponi G. and Williams R.J.P. (1992) Three-dimensional structure of acylphosphatase. Refinement and structure analysis. J. Mol. Biol. 224: 427−440
- Π Π΅ΠΊ S.B., Usami M., Bilir N., Fischer-Bovenkerk C., Ueda T. (1990) Protein phosphorylation in pancreatic islets induced by 3-phosphoglycerate and 2-phosphoglycerate. Proc. Natl. Acad. Sci. USA 87(11): 4294−8
- Pohl E., Brunner N., Wilmanns M., Hensel R. (2002) The crystal structure of the allosteric non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase from the hyperthermophilic archaeum Thermoproteus tenax. J. Biol. Chem. 277(22): 19 938−45
- Ramponi G., Liguri G., Nediani C., Stefani M., Taddei N., Nassi P. (1988) Acylphosphatase increases the rate of ethanol production from glucose in cell-free extracts of Saccharomyces cerevisiae. Biotechnol. Appl. Biochem. 10(5): 408−13
- Ramponi G. (1975) 1,3-diphosphoglycerate phosphatase. Methods Enzymol. 42: 409−426
- Raugei, G., Modesti, A., Magherini, F., Marzocchini, R., Vecchi, M., and Ramponi, G. (1996) Expression of acylphosphatase in Saccharomyces cerevisiae enhances ethanol fermentation rate. Biotechnol. Appl. Biochem. 23: 273−278
- Ravichandran V., Seres Π’., Moriguchi Π’., Thomas J.A., and Johnston R.B., Jr. (1994) S-Thiolation of glyceraldehyde-3-phosphate dehydrogenase induced by the phagocytosis-associated respiratory burst in blood monocytes. J. Biol. Chem. 269: 25 010−25 015
- Rosenberg L.L., Arnon D.I. (1955) The preparation and properties of a new glyceraldehyde-3-phospate dehydrogenase from photosynthetic tissues. J. Biol. Chem. 217: 361−371
- Saudek V., Atkinson R.A., Williams R.J.P. and Ramponi G. (1989) Identification and description of a-helical regions in horse muscle acylphosphatase by .H nuclear magnetic reso-nance spectroscopy. J. Mol. Biol. 205: 229−239
- Saudek V., Williams R.J.P. and Ramponi G. (1988) Secondary structure of acylphosphatase from rabbit skeletal muscle. A nuclear magnetic resonance study. J. Mol. Biol. 199: 233−237
- Saudek V., Wormald M.R., Williams R.J.P., Boyd J., Stefani M. and Ramponi G. (1989) Identification and description of (3-structure in horse muscle acylphosphatase by nuclear magnetic resonance spectroscopy. J. Mol. Biol. 207: 405−415
- Scagliarini S., Trost P., Valenti V., Pupillo P. (1990) Glyceraldehyde-3-phosphate: NADP+ reductase of spinach leaves. Plant Physiol. 94: 1337−1344
- Schmalhausen E.V., Muronetz V.I., Nagradova N.K. (1997) Rabbit muscle GAPDH: non-phosphorylating dehydrogenase activity induced by hydrogen peroxide. FEBS Lett. 414(2): 247−52
- Schmalhausen E.V., and Muronetz V.I. (1997) An uncoupling of the processes of oxidation and phosphorylation in glycolysis. Biosci. Rep. 17: 521−527
- Schmalhausen E.V., Nagradova N.K., Boschi-Muller S., Branlant G., and Muronetz V.I. (1999) Mildly oxidized GAPDH: the coupling of the dehydrogenase and acyl phosphatase activities. FEBS Lett. 452: 219−222
- Schuppe-Koistinen I., Moldeus P., Bergman Π’., and Cotgreave I.A. (1994) S-Thiolation of human endothelial cell glyceraldehyde-3 -phosphate dehydrogenase after hydrogen peroxide treatment. Eur. J Biochem. 221: 1033−1037
- Schweins Π’., Geyer M., Scheffzek K., Warshel A., Kalbitzer H. R. and Wittinghofer A. (1995) Substrate-assisted catalysis as a mechanism for GTP hydrolysis of p21 ras and other GTP-binding proteins. Nature Struct. Biol. 2: 36−44
- Schweins Π’., Langen R. and Warshel A. (1994) Why have mutagenesis studies not located the general base in ras p21? Nature Struct. Biol. 1: 476−484
- Scopes R.K., and Stoter A. (1982) Purification of all glycolytic enzymes from one muscle extract. Methods in Enzymology 90: 479−491
- Servaites J.C., Geiger D.R., Tucci M.A., Fondy D.R. (1989) Leaf carbon metabolism and metabolite levels during a period of sinusoidal light. Plant Physiol 89: 403−408
- Sheikh S., Ni L., Hurley T.D., Weiner H. (1997) The potential roles of the conserved amino acids in human liver mitochondrial aldehyde dehydrogenase. J. Biol. Chem. 272(30): 18 817−22
- Sheikh S, Ni L., Weiner H. (1997) Mutation of the conserved amino acids of mitochondria aldehyde dehydrogenase. Role of the conserved residues in the mechanism of reaction. Adv. Exp. Med. Biol. 414:195−200
- Siebers Π., Klenk H.P., Hensel R. (1998) PPi-dependent phosphofructokinase from Thermoproteus tenax, an archaeal descendant of an ancient line in phosphofructokinase evolution. J. Bacterid. 180(8): 2137−43
- Solti M., Friedrich P. (1979) The «enzyme-probe» method for characterizating metabolite pools. The use of NAD-glycohydrolase in human erythrocyte sonicate as a model system. Eur. J. Biochem. 95: 551 559
- Sophos N.A., Pappa A., Ziegler T.L., Yasiliou V. (2001) Aldehyde dehydrogenase gene superfamily: the 2000 update. Chemico-Biological Interactions 130−132: 323−337
- Stefani M. and Ramponi G. (1995) Acylphosphate phospho-hydrolases. Life Chem. Rep. 12: 271−301
- Stefani M., Taddei N. and Ramponi G. (1997) Insights into acylphosphatase structure and catalytic mechanism. Cell. Mol. Life Sci. 53:141−151
- Steinmetz C.G., Xie P., Weiner H., Hurley T.D. (1997) Structure of mitochondrial aldehyde dehydrogenase: the genetic component of ethanol aversion. Structure 5(5): 701−11
- Steinmetz C.G., Xie P., Weiner H., Hurley D.T. (1997) Structure of mitochondrial aldehyde dehydroge-nase: the genetic component of ethanol aversion. Structure 5: 701−711
- Stock A. (1999) Biophysics. Relating dynamics to function. Nature 400(6741): 221−2
- Szewczuk K., Wolny H., Baranowsky T. (1961) Nova metoda otrzyzmywania D-glyceraldehydo-fosforany. Acta Bioch. Polon. 8: 201 209
- Taddei N., Stefani M., Magherini F., Chiti F., Modesti A., Raugei G. et al. (1996) Looking for residues involved in the muscle acylphosphatase catalytic mechanism and structural stabilization: role of Asn41, Thr42 and Thr46. Biochemistry 35: 7077−7083
- Thomas S.M. and Rees T. (1972) Glycolysis during gluconeogenesis in cotyledons of Cucurbita pepo. Phytochemistry 11: 2187−2194
- Thunnissen M.M., Taddei N., Liguri G., Ramponi G., Nordlund P. (1997) Crystal structure of common type acylphosphatase from bovine testis. Structure 5(1): 69−79
- Tisdale E.J. (2002) Glyceraldehyde-3-phosphate dehydrogenase is phosphorylated by protein kinase CiJX and plays a role in microtubule dynamics in the early secretory pathway. J. Biol. Chem. 277(5): 33 343 341
- Tsou C.L. (1993) Conformational flexibility of enzyme active sites. Science. 262(5132): 380−1
- Ueda Π’., Plagens D.G. (1987) Phosphoglycerate-dependent protein phosphorylation. Proc. Natl. Acad. Sci. USA 84(5): 1229−33
- Valenti V., Scagliarini S., Pupillo P. (1986) The distribution of some NADP-linked dehydrogenases in photosynthetic tissues of maize leaves. J. Experimental Botany 37: 606−614
- Vasiliou V., Pappa A., Petersen D. R. (2000) Role of aldehyde dehydrogenases in endogenous and xenobiotic metabolism. Chemico-Biological Interactions 129: 1−19
- Vedadi M., Meighen E. (1997) Critical glutamic acid residues affecting the mechanism and nucleotide specificity of Vibrio harveyi aldehyde dehydrogenase. Eur. J. Biochem. 246(3): 698−704
- Verhees C.H., Tuininga J.E., Kengen S.W., Stams A.J., van der Oost J., de Vos W.M. (2001) ADP-dependent phosphofructokinases in mesophilic and thermophilic methanogenic archaea. J. Bacteriol. 183(24): 7145−53.
- Wang X., Weiner H. (1995) Involvement of glutamate 268 in the active site of human liver mitochondrial (class 2) aldehyde dehydrogenase as probed by site-directed mutagenesis. Biochemistry 34(1): 237−43
- Wang X., Weiner H. (1995) Involvement of glutamate 268 in the active site of human liver mitochondrial (class 2) aldehyde dehydrogenase as probed by site-directed mutagenesis. Biochemistry 34: 237−243
- Yoshida A., Rzhetsky A., Hsu C. and Chang C. (1998) Human aldehyde dehydrogenase gene family. Eur. J. Biochem. 251: 549−557
- Zidek L., Novotny M.V., Stone M.J. (1999) Increased protein backbone conformational entropy upon hydrophobic ligand binding. Nature Struct. Biol. 6(12): 1118−211. ΠΠ»Π°Π³ΠΎΠ΄Π°ΡΠ½ΠΎΡΡΠΈ
- ΠΠ»Π°Π³ΠΎΠ΄Π°ΡΡ ΡΠ²ΠΎΡ ΡΠ΅ΠΌΡΡ ΠΈ ΠΎΡΠ΄Π΅Π»ΡΠ½ΠΎ ΡΡΠΏΡΡΠ³Ρ (ΡΠ°ΠΊΠΆΠ΅ ΡΠΎΡΡΡΠ΄Π½ΠΈΡΡ ΠΎΡΠ΄Π΅Π»Π°) ΠΠΈΡΠ½ΠΈΠ²Π΅ΡΠΊΡΡ (ΠΡΡΡΡΠ½ΠΎΠ²Ρ) ΠΠ»Π΅Π½Ρ ΠΠ²Π°Π½ΠΎΠ²Π½Ρ Π·Π° ΠΏΠΎΡΡΠΎΡΠ½Π½ΠΎΠ΅ Π²Π½ΠΈΠΌΠ°Π½ΠΈΠ΅ ΠΈ ΠΏΠΎΠΌΠΎΡΡ.
- ΠΡΠΎΠΌΠ΅ ΡΠΎΠ³ΠΎ, Ρ Π±Π»Π°Π³ΠΎΠ΄Π°ΡΡ ΡΠΎΡΡΡΠ΄Π½ΠΈΠΊΠΎΠ² ΠΎΡΠ΄Π΅Π»Π° ΡΠΈΠ·ΠΈΡΠ΅ΡΠΊΠΈΡ ΠΌΠ΅ΡΠΎΠ΄ΠΎΠ² ΠΈΠ·ΠΌΠ΅ΡΠ΅Π½ΠΈΠΉ ΠΠΠ Π€Π₯Π ΠΈΠΌ. ΠΠ΅Π»ΠΎΠ·Π΅ΡΡΠΊΠΎΠ³ΠΎ ΠΠΠ£ ΠΡΠ»ΠΎΠ²Π° Π. Π., ΠΠΈΡΡΡΠΈΠ½Ρ Π. Π. ΠΈ ΠΠΎΠΏΡΠ»ΠΎΠ²Π° Π‘. Π. Π·Π° ΠΏΠΎΠΌΠΎΡΡ Π² Π²ΡΠΏΠΎΠ»Π½Π΅Π½ΠΈΠΈ ΡΠΊΡΠΏΠ΅ΡΠΈΠΌΠ΅Π½ΡΠΎΠ² ΠΏΠΎ ΡΠΊΠ°Π½ΠΈΡΡΡΡΠ΅ΠΉ ΠΊΠ°Π»ΠΎΡΠΈΠΌΠ΅ΡΡΠΈΠΈ.
- Π‘ΠΏΠ°ΡΠΈΠ±ΠΎ ΡΠ°ΠΊΠΆΠ΅ ΠΡΠ°ΠΌΠ°ΡΠΎΠ²ΠΎΠΉ Π’. Π. (Stockholm University, Sweden) Π·Π° ΠΏΠΎΠΌΠΎΡΡ Π² ΠΏΠΎΠ»ΡΡΠ΅Π½ΠΈΠΈ ΡΡΠ΄Π° ΠΏΠΎΠ»Π½ΡΡ ΡΠ΅ΠΊΡΡΠΎΠ² ΡΡΠ°ΡΠ΅ΠΉ.