Phosphatase Fold Rhodanese - Revision history

Gerard: /* Not all rhodanese domains have phosphatase activity */

2016-09-07T18:31:01Z

‎Not all rhodanese domains have phosphatase activity

Gerard: /* Not all rhodanese domains have phosphatase activity */

2016-09-07T18:30:18Z

‎Not all rhodanese domains have phosphatase activity

Gerard at 01:50, 23 August 2015

2015-08-23T01:50:52Z

Gerard at 01:49, 23 August 2015

2015-08-23T01:49:49Z

Gerard: /* Not all rhodanese domains have phosphatase activity */

2015-08-23T01:27:30Z

‎Not all rhodanese domains have phosphatase activity

Gerard at 01:26, 23 August 2015

2015-08-23T01:26:49Z

Gerard at 01:26, 23 August 2015

2015-08-23T01:26:13Z

Mark: Mark moved page Phosphatase Fold Rhodanase to Phosphatase Fold Rhodanese over redirect

2015-01-01T03:34:44Z

Mark moved page Phosphatase Fold Rhodanase to Phosphatase Fold Rhodanese over redirect

Mark: Mark moved page Phosphatase Fold Rhodanese to Phosphatase Fold Rhodanase

2015-01-01T03:33:58Z

Mark moved page Phosphatase Fold Rhodanese to Phosphatase Fold Rhodanase

Mark at 23:18, 31 December 2014

2014-12-31T23:18:28Z

@@ Line 11: / Line 11: @@
 Rhodanese domains are ubiquitous structural domains found in both eukaryotes and prokaryotes. It is named after bovine liver rhodanese, the most well characterized sulfurtranferase. The fold and its single superfamily consists of at least ten families based on different domain combinations <cite>bordo02</cite>. The member proteins have various functions and physiological substrates, such as, thiosulfate:cyanide sulfurtransferase, protein phosphatase, and arsenate reductase. The cysteine at catalytic site is necessary for its activity no matter what its substrate is. But, whether the functional specificity is determined solely by catalytic motif is unknown, though it seems different families have different catalytic motif in length and conserved residues <cite>bordo02</cite>.
-Curiously, rhodanese domains are found as accessory domains in some [[Phosphatase_Family_DSP|dual-specificity phosphatases]] of the [[Phosphatase_Fold_CC1|CC1 fold]]. All of these have the catalytic cysteine replaced by aspartate or glutamate, and are believed to be catalytically inactive.
+Rhodanese domains are found as accessory domains in some [[Phosphatase_Family_DSP|dual-specificity phosphatases]] of the [[Phosphatase_Fold_CC1|CC1 fold]]. All of these have the catalytic cysteine replaced by aspartate or glutamate, and are believed to be catalytically inactive.
 === Reference ===

@@ Line 9: / Line 9: @@
 ===== Not all rhodanese domains have phosphatase activity =====
-Rhodanese domains are ubiquitous structural domains found in both eukaryotes and prokaryotes. It is named after bovine liver rhodanese, the most well characterized sulfurtranferase. The fold and its single superfamily consists of at least ten families based on different domain combination <cite>bordo02</cite>. The member proteins have various functions and physiological substrates, such as, thiosulfate:cyanide sulfurtransferase, protein phosphatase, and arsenate reductase. The cysteine at catalytic site is necessary for its activity no matter what its substrate is. But, whether the functional specificity is determined solely by catalytic motif is unknown, though it seems different families have different catalytic motif in length and conserved residues <cite>bordo02</cite>.
+Rhodanese domains are ubiquitous structural domains found in both eukaryotes and prokaryotes. It is named after bovine liver rhodanese, the most well characterized sulfurtranferase. The fold and its single superfamily consists of at least ten families based on different domain combinations <cite>bordo02</cite>. The member proteins have various functions and physiological substrates, such as, thiosulfate:cyanide sulfurtransferase, protein phosphatase, and arsenate reductase. The cysteine at catalytic site is necessary for its activity no matter what its substrate is. But, whether the functional specificity is determined solely by catalytic motif is unknown, though it seems different families have different catalytic motif in length and conserved residues <cite>bordo02</cite>.
 Curiously, rhodanese domains are found as accessory domains in some [[Phosphatase_Family_DSP|dual-specificity phosphatases]] of the [[Phosphatase_Fold_CC1|CC1 fold]]. All of these have the catalytic cysteine replaced by aspartate or glutamate, and are believed to be catalytically inactive.

← Older revision		Revision as of 01:50, 23 August 2015
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	[[Phosphatase classification\|Phosphatase Classification]]: [[Phosphatase_Fold_Rhodanese\|Fold Rhodanese]]		[[Phosphatase classification\|Phosphatase Classification]]: [[Phosphatase_Fold_Rhodanese\|Fold Rhodanese]]
−

	Fold CC3 (Rhodanese) has a single superfamily [[Phosphatase_Superfamily_Rhodanese\|CC3 (Rhodanese)]].		Fold CC3 (Rhodanese) has a single superfamily [[Phosphatase_Superfamily_Rhodanese\|CC3 (Rhodanese)]].

@@ Line 6: / Line 6: @@
 Fold CC3 (Rhodanese) has a single superfamily [[Phosphatase_Superfamily_Rhodanese|CC3 (Rhodanese)]].
-The CC3 (Cys-based group III) phosphatase superfamily has rhondanese fold catalytic domain, which has the Cx5R catalytic motif shared with the [[Phosphatase_Superfamily_CC1| CC1]] and [[Phosphatase_Superfamily_CC2|CC2]] folds. This fold encodes enzymes with a number of redox functions, of which only the  [[Phosphatase_Family_CDC25|CDC25 family]] has protein phosphatase activitiy.
+The CC3 (Cys-based group III) phosphatase superfamily has rhodanese fold catalytic domain, which has the Cx5R catalytic motif shared with the [[Phosphatase_Superfamily_CC1| CC1]] and [[Phosphatase_Superfamily_CC2|CC2]] folds. This fold encodes enzymes with a number of redox functions, of which only the  [[Phosphatase_Family_CDC25|CDC25 family]] has protein phosphatase activitiy.
 ===== Not all rhodanese domains have phosphatase activity =====

@@ Line 12: / Line 12: @@
 Rhodanese domains are ubiquitous structural domains found in both eukaryotes and prokaryotes. It is named after bovine liver rhodanese, the most well characterized sulfurtranferase. The fold and its single superfamily consists of at least ten families based on different domain combination <cite>bordo02</cite>. The member proteins have various functions and physiological substrates, such as, thiosulfate:cyanide sulfurtransferase, protein phosphatase, and arsenate reductase. The cysteine at catalytic site is necessary for its activity no matter what its substrate is. But, whether the functional specificity is determined solely by catalytic motif is unknown, though it seems different families have different catalytic motif in length and conserved residues <cite>bordo02</cite>.
-Curiously, rhodanese domains are found as accessory domains in some [[Phosphatase_Family_DSP|dual-specificity phosphatases]] of the [[Phosphatase_Superfamily_CC1|CC1 superfamily]]. All of these have the catalytic cysteine replaced by aspartate or glutamate, and are believed to be catalytically inactive.
+Curiously, rhodanese domains are found as accessory domains in some [[Phosphatase_Family_DSP|dual-specificity phosphatases]] of the [[Phosphatase_Fold_CC1|CC1 fold]]. All of these have the catalytic cysteine replaced by aspartate or glutamate, and are believed to be catalytically inactive.
 === Reference ===

← Older revision	Revision as of 03:34, 1 January 2015
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← Older revision	Revision as of 03:33, 1 January 2015
(No difference)

← Older revision		Revision as of 23:18, 31 December 2014
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	__NOTOC__		__NOTOC__

−	[[Phosphatase classification\|Phosphatase Classification]]: [[Phosphatase_Fold_Rhodanese\|Fold Rhodanese]]:	+	[[Phosphatase classification\|Phosphatase Classification]]: [[Phosphatase_Fold_Rhodanese\|Fold Rhodanese]]